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Professor Laura Na Liu Wins 2019 Nano Letters Young Investigator Lectureship Award

Nano Letters and the ACS Division of Colloid & Surface Chemistry are proud to announce Professor Laura Na Liu, Heidelberg University, as the winner of the 2019 Nano Letters Young Investigator Lectureship Award. The award honors the contributions of a young investigator who has made major impacts on the field of nanoscience and nanotechnology.

Throughout her career, Professor Liu has contributed numerous key papers that have shaped the fields of nanophotonics, metamaterials, and DNA nanotechnology. Her research has also led to the creation of new fields, including DNA-enabled dynamic nanoplasmonics.

With over 11,000 citations and an average of almost 200 citations per article, it’s no wonder that Professor Liu is viewed as a highly respected researcher. She is known for producing sound results and carefully listing the methods and protocols in her papers so others can easily reproduce the research.

The quality of Professor Liu’s work is also evident in the various awards she’s won throughout her career, including the Light 2015 Young Woman in Photonics Award, the IUPAP Young Scientist Prize in Optics, the Kavli Foundation Early Career Award and the prestigious Rudolph-Kaiser prize, to name a few.

Professor Liu will be presenting her research at a symposium and award ceremony during the 2020 ACS Spring National Meeting in Philadelphia. In the meantime, here are some of her recent articles published in Nano Letters:

Dynamic Plasmonic System That Responds to Thermal and Aptamer-Target Regulations
Nano Lett., 2018, 18 (11), pp 7395–7399
DOI: 10.1021/acs.nanolett.8b03807

Dynamic Janus Metasurfaces in the Visible Spectral Region
Nano Lett., 2018, 18 (7), pp 4584–4589
DOI: 10.1021/acs.nanolett.8b01848

Dynamic Color Displays Using Stepwise Cavity Resonators
Nano Lett., 2017, 17 (9), pp 5555–5560
DOI: 10.1021/acs.nanolett.7b02336

ACS Editors Share Their Favorite Advice

Behind every great scientist is a mentor who helped point them in the right direction and gave them sage advice. ACS Publications Editors are no different. Each of them received insights early in their careers that stuck with them and helped make them the successful chemists they are today. In this video, ACS Publications Editors share the best professional advice they’ve received over the years, covering topics as diverse as their approaches to research, dealing with competition, and staying plugged into the scientific community.

ACS Editors Share Their Favorite Advice

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The ASC Publications Editors featured in the video are (in order of appearance): Professor Shana Sturla, Editor-in-Chief of Chemical Research in Toxicology; Professor Patrick Sexton, Editor-in-Chief of ACS Pharmacology & Translational Science; Professor Cynthia J. Burrows Editor-in-Chief of Accounts of Chemical Research; ProfessorLuis Liz-Marzán, Associate Editor of ACS Nano; Professor Kai Rossen Editor-in-Chief of Organic Process Research & Development.

Share the best professional advice you’ve ever received in the comments.

Tracking Individual Flu Viruses Shows the Antiviral Drug Zanamivir in Action

Blame the flu’s infectivity on these two proteins: hemagglutinin (HA), which enables the virus to stick to cells and enter them, and neuraminidase (NA), which cleaves HA bonds to help viral progeny detach from cells to find and invade new ones. A new combination of analytical techniques now offers a way to count how many interactions a single virus’s surface proteins have with cell surface sugars—and reveals an unexpected effect of zanamivir, a common flu medication. The results offer a route to better understand viral infectivity and could aid in designing new drug molecules.

Flu strains such as H5N1 or H3N2 are named and characterized for the specific HA and NA variants they carry. Although a single HA bond with a receptor is weak, each virus particle forms many such bonds. To infect a cell, multiple HA molecules must bind with sialic acid–containing receptors on the cell surface. Previous studies have determined the average strength and number of bonds a virus makes by measuring, for example, the overall force required to detach a virus from a cell. But these techniques don’t reveal the strength of each individual bond or how dynamic it might be.

To get a more accurate picture of the bonds formed by a single virus, Stephan Block of the Free University of Berlin and his colleagues turned to a combination of techniques: single-particle tracking, which uses real-time imaging to track fluorescent-labeled viruses, and total internal reflection fluorescence microscopy. They created a lipid bilayer containing cell surface receptors to mimic a cell and poured fluorescent-labeled H3N2 virus particles over this layer. The microscopy tracked when particles bound or detached from the surface, and single-particle tracking monitored random viral movements caused by diffusion. Together, the two assays directly observe how many bonds a virus makes with a given cell at a particular moment in time, Block says.

The combination of methods is a “clever experimental design,” says Ravi Kane, who studies the interactions of nanostructures and biological systems at Georgia Tech and was not involved in the study. The study “breaks a complex situation up into simpler pieces,” he says, so researchers can dissect virus-receptor interactions on a fine scale.

The researchers also analyzed the effects of the antiviral drug zanamivir, which is known to block NA activity and thus prevent budding viruses from escaping one cell to infect others. They found that the drug also increased the rate of attachment of viruses to the membrane, keeping viral particles stuck to the membrane longer. The effect was “surprising to me,” Block says, because NA inhibitors are largely studied for their effects on virus egress, not attachment.

Why this occurs is unclear, though it’s possible the effect may be because once NA is inhibited by the drug, it’s unavailable to cleave HA–sialic acid bonds, Kane suggests.

Such studies could help understand relationships between the infectivity of viruses and how they bind or detach and also reveal how different cell-surface proteins or sugars might alter a virus’s response to drugs. Understanding how HA and NA work in concert within a single viral particle can help scientists figure out the full range of virus-cell interactions. Jacob Martin, a postdoctoral researcher at the Massachusetts Institute of Technology, says that “when fighting a pathogen, it’s interesting to know the range of its capabilities, which could affect how different drugs might prevent infections.”

This article is reproduced with permission from C&EN (© American Chemical Society). The article was first published on February 25, 2019.

Marjory Stephenson: Founder of Microbial Biochemistry

Marjory Stephenson was one of the few scientists who discovered a whole new field of research. The historian of biochemistry, Robert Kohler, has shown that the study of bacterial biochemistry was, in large part, defined by the work of Stephenson1. In this account, we endeavor to encompass highlights of her personal life and research work. For a more detailed description of her research work, we direct the reader to authoritative professional obituaries, such as those by Muriel Robertson2 and by Donald Woods3. The recent biography by Soňa Štrbáňová4 contains a much fuller account of Stephenson’s life and work.

Early Life

Stephenson was born 24 January 1885 at Burwell, a village near Cambridge, and she spent most of her life there. Her parents were mother Sarah Rogers and father Robert Stephenson, who was a farmer. Marjory Stephenson was more than eight years younger than the next youngest of her three siblings. She remarked how this age difference influenced her life:

Owing to position in my family, almost an ‘only child’ and somewhat of a little prig, I acquired a childish interest in science from my beloved governess [Anna Jane Botwright] and later from my father. I remember … hearing the facts of symbiotic nitrogen fixation from my father as we crossed a clover field [age about 10]5

Educated by a governess until the age of twelve, Stephenson then received a scholarship to attend the Berkhamsted High School for Girls6. After completing her secondary schooling at Berkhamsted, Stephenson’s mother insisted that she obtain a university education. Furthermore, her mother decided that Newnham College, a women’s college of the University of Cambridge, was where Marjory should go, just as her elder sister (Alice Mary) had done 14 years earlier to study history.

At Newnham College

Newnham College was founded in 1875 as the second women’s college of Cambridge University (the first being Girton). Located on the edge of the city of Cambridge, Newnham became more prominent for science than did Girton. Arriving at Newnham in 1903, Stephenson studied chemistry, physiology, and zoology. During those times, students at the Cambridge women’s colleges led separate and sheltered lives from the (male) university. For example, women students were not allowed to enter the University Science Laboratories. Instead, they were required to use the Balfour Biological Laboratory for Women7 and Newnham’s own Chemistry Laboratory.

For chemistry, Stephenson was taught by the Newnham Lecturer in Chemistry, Ida Freund (1863–1914)8. Freund was the charismatic figure in chemistry at Newnham from 1890 to 19129. An earlier Newnham student, Catherine Holt, in a letter to her mother, had commented on Freund:

I attended my first lecture today; it was Chemistry; … Afterwards we adjourned for a couple of hours to the laboratory here; Miss Freund is the presiding genius, a jolly, stout German, whose clothes are falling in rags off her back. We made lots of horrible smells and got back here for lunch at a quarter past one10.

Though women students had been admitted to Cambridge University, they were barred from being formally granted degree status (this was not permitted until 1948). Instead, Stephenson, like the other women students of the time, had to be satisfied with taking and passing the final examination, called the Tripos11. She satisfactorily completed the Part I Natural Sciences Tripos in 1906.

Read the full chapter.

References:
1. Kohler R. E. Innovation in Normal Science: Bacterial Physiology Isis. 1985 76 162 181.
2. Robertson M. Marjory Stephenson. 1885–1948 Obit. Notices Fellows Roy. Soc. 1949 6 563 577.
3. Woods D. D. Marjory Stephenson Biochem. J. 1950 46 377 383.
4. Štrbáňová, S. Holding Hands with Bacteria: The Life and Work of Marjory Stephenson. Springer: Berlin, Germany, 2016.
5. Stephenson M. Personal Records, Royal Society, cited in Mason, J. The Admission of the First Women to the Royal Society of London Notes Records R. Soc. London 1992 46 284 285.
6. Williams, B. H. G. Berkhamsted School for Girls: A Centenary History 1888–1988. Hazel Watson and Viney: Aylesbury, England, 1988.
7. Richmond M. L. A Lab of One’s Own: The Balfour Biological Laboratory for Women at Cambridge University, 1884–1914 Isis.1997 88 422 455.
8. Mason, J. Marjory Stephenson 1885–1948. In Cambridge Women: Twelve Portraits; Shils, E. and Blacker, C. , Eds.; Cambridge University Press: Cambridge, England, 1996; p 115.
9. Wilson, H. Miss Freund. In A Newnham Anthology [2nd Ed.]; Phillips, A. , Ed.; Newnham College: Cambridge, England, 1988; pp 71– 72.
10. Letter, Holt, C. D. to Holt, L. , 12 October 1889. In Letters from Newnham College 1889–1892; Cockburn, E. O. , Ed.; Newnham College, Cambridge, England; 1987; p 11.
11. Tullberg, R. McW. Women at Cambridge; Cambridge University Press: Cambridge, England, 1998; p 66.

This post is an excerpt from ‘Marjory Stephenson: Founder of Microbial Biochemistry‘, The Posthumous Nobel Prize in Chemistry. Volume 2. Ladies in Waiting for the Nobel Prize.
Chapter Authors: M. F. Rayner-Canham, G. W. Rayner-Canham
Volume Editors: Vera V. Mainz, E. Thomas Strom
Publication Date (Web): December 14, 2018
Copyright © 2018 American Chemical Society

ACS Editors’ Choice: Unprecedented Ultralow Detection Limit of Amines — and More!

This week: Unprecedented ultralow detection limit of amines — and more!

Each and every day, ACS grants free access to a new peer-reviewed research article from one of the Society’s journals. These articles are specially chosen by a team of scientific editors of ACS journals from around the world to highlight the transformative power of chemistry. Access to these articles will remain open to all as a public service.

Check out this week’s picks!
***
Antimonite Complexation with Thiol and Carboxyl/Phenol Groups of Peat Organic Matter

Environ. Sci. Technol., Article ASAP
DOI: 10.1021/acs.est.9b00495
***
Secreted Protein Acidic and Rich in Cysteine Mediated Biomimetic Delivery of Methotrexate by Albumin-Based Nanomedicines for Rheumatoid Arthritis Therapy

ACS Nano, Article ASAP
DOI: 10.1021/acsnano.9b01710

***
Unprecedented Ultralow Detection Limit of Amines using a Thiadiazole-Functionalized Zr(IV)-Based Metal–Organic Framework

J. Am. Chem. Soc., Article ASAP
DOI: 10.1021/jacs.9b01839
***
Tailoring the Antimicrobial Response of Cationic Nanocellulose-Based Foams through Cryo-Templating

ACS Appl. Bio Mater., Article ASAP
DOI: 10.1021/acsabm.9b00034
***
An Inter-Laboratory Study of Zn–Sn–Ti–O Thin Films using High-Throughput Experimental Methods

ACS Comb. Sci., Article ASAP
DOI: 10.1021/acscombsci.8b00158
***
Nonpentacene Polarizing Agents with Improved Air Stability for Triplet Dynamic Nuclear Polarization at Room Temperature

J. Phys. Chem. Lett., 2019, 10, pp 2208–2213
DOI: 10.1021/acs.jpclett.9b00480
***
Dual-Sized Microparticle System for Generating Suppressive Dendritic Cells Prevents and Reverses Type 1 Diabetes in the Nonobese Diabetic Mouse Model

ACS Biomater. Sci. Eng., Article ASAP
DOI: 10.1021/acsbiomaterials.9b00332
***
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Sulfur-Based Polymer Transmits Long-Wavelength Infrared Better Than Any Other Known Plastic

A sulfur-based polymer that can transmit light at long infrared wavelengths could enable a new class of lightweight plastic optics—as long as scientists can figure out how to reliably make it.

The polymer allows light at wavelengths from 7.4 to 14 µm to pass. Thermal imaging devices, similar to night-vision goggles, use those wavelengths to detect heat signatures, allowing the military to identify targets and vehicles in darkness. Lenses and waveguides for devices that operate at those wavelengths are normally made from chalcogenide glasses containing sulfur, selenium, or tellurium, or from other IR-transparent materials such as germanium or crystalline silicon. Those kinds of optics are all heavier and more expensive than plastic optics would be and require more energy to make.

“I can’t find evidence in the literature that there’s a polymer that transmits this far into the long-wave infrared at these thicknesses,” says Darryl A. Boyd, a chemist in the optical sciences division of the US Naval Research Laboratory who led the work. Whereas most polymers thicker than about 1 mm are opaque at such wavelengths, his team’s material was transparent at thicknesses greater than 1.5 mm. It also showed a high index of refraction; lenses made from high-index materials have high focusing power, which means that a thinner lens can achieve the same focus as a thicker lens with a lower index. In organic polymers, the refractive index rarely exceeds 1.7, but Boyd and his team measured an index of 1.98 with 636.4 nm (red) wavelength light and 1.94 with 1548.4 nm (near-infrared) light.

The team created their material using a fairly new process called inverse vulcanization. Standard vulcanization involves strengthening a carbon polymer backbone with sulfur cross-linking; in inverse vulcanization, a sulfur polymer is the backbone and carbon the cross-linker. Boyd’s team stirred tetravinyltin into molten sulfur and then cured it for three to four hours at 125 to 130 °C. Boyd says this is the first time an organometallic compound has been used in inverse vulcanization and is, therefore, an early attempt to discern how a metal may affect the optical, thermal, or mechanical properties of the polymer.

The material started out rubbery but became brittle within a day, for reasons Boyd hasn’t figured out yet. He says he plans to pursue that question, as well as try the same synthesis method with compounds that have a metal other than tin to compare the resulting properties. The change in consistency is an important problem to solve for the materials to be useful for optics, Boyd says. Another processing issue is that the polymer contained some trapped bubbles, which outgassed over the course of a few days, leaving behind voids that would distort an image.

Jeffrey Pyun, a chemist at the University of Arizona who pioneered inverse vulcanization, calls the paper “the beginnings of a really good finding” but wants to see more work to characterize the structure of the polymer to validate that the material turned out to be what was expected. Using polymers for long-wave infrared optics is a new and challenging application, though, and this paper points in a promising direction, he says.

Tom Hasell of the University of Liverpool says more work needs to be done in understanding and processing these materials, but finds the work promising. “There is no denying that this is a great result,” he says, “but I think it shows more what is possible than what has been fully realized yet.” He adds that there’s still a lot of work to be done to improve the material to the point where it can make defect-free, damage-resistant lenses.

This article is reproduced with permission from C&EN (© American Chemical Society). The article was first published on February 20, 2019.

Exploring Hot Topics in Proteomics

An April 10 Journal of Proteome Research webinar, “Hot Topics in Proteomics” highlighted perspectives from three leading scientists in three important and rapidly developing areas of proteomics, including precision medicine, precision proteomics, single-cell proteomics. The webinar is moderated by John Yates, the Editor-in-Chief of Journal of Proteome Research and Professor at the Scripps Research Institute. Each topic is based on a recently published perspective from the Journal of Proteome Research.

Transformative Opportunities for Single-Cell Proteomics

Nikolai Slavov (Assistant Professor, Bioengineering, Northeastern University) studies post-transcriptional regulation during cell differentiation, with a focus on translational regulation by specialized ribosomes. His group also develops and applies single-cell mass-spectrometry methods for investigating post-transcriptional regulation in single cells. He speaks on recent developments in single cell proteomics that hold promise to enable participation in projects such as the human cell atlas.

Proteome-Wide Structural Biology: An Emerging Field for the Structural Analysis of Proteins on the Proteomic Scale

Lisa Jones (Ph.D., Assistant Professor of Pharmaceutical Sciences, School of Pharmacy, University of Maryland) is an expert in the field of structural proteomics. Her research focuses on the development and application of in vivo hydroxyl radical footprinting methods to study protein conformations and interactions. She speaks about mass spectrometry-based protein footprinting for analysis of protein interactions and dynamics. As the U.S. population ages, protein misfolding diseases associated with aging are on the rise. These methods will help us better understand these diseases.

Precision Medicine: Role of Proteomics in Changing Clinical Management and Care:

Jennifer VanEyk (Ph.D., Director, Advanced Clinical Biosystems Institute in the Department of Biomedical Sciences) is an international leader in the area of clinical proteomics and her lab focuses on developing technical pipelines for de novo discovery and large scale quantitative mass spectrometry methods. She speaks on precision proteomics and their role in precision medicine and personalized health. In order to fashion better and more personalized medicine, we must understand what it is that makes us unique as individuals. Precision proteomics will play a vital role in this effort.


Access the on-demand webinar and learn more about the speakers and research areas such as precision medicine, precision proteomics, single-cell proteomics, personalized medicine, and personalized health.

ACS Materials Letters Launches Free Summit Series in China

Bin Liu, Deputy Editor of ACS Materials Letters

Earlier this year ACS Publications announced and launched ACS Materials Letters, a new journal publishing the most cutting-edge and urgent results at the forefront of fundamental and applied materials research. To introduce the journal, Bin Liu, Deputy Editor of ACS Materials Letters, will be visiting various universities in China throughout May for the ACS Materials Letters Summit Series. At these events, Liu will be discussing the journal’s mission, how to publish in the journal, and the editorial team’s dedication to fast processing times.

In addition, each visit will include a series of talks from some of China’s most elite materials scientists, who will be presenting the latest groundbreaking and emerging research. See below for the full Summit schedule, including the speakers and their topics, location, times, and how to register to attend these free events.

Wednesday, May 15, Hong Kong University of Science and Technology

Hosted by: Professor Ben Zhong Tang, South China University of Technology

Agenda:

8:15 a.m. – 8:45 a.m

Registration

8:45 a.m. – 9:00 a.m.

Professor Bin Liu, ACS Materials Letters Deputy Editor, National University of Singapore

Opening Remarks & Presentation on ACS Materials Letters

9:00 a.m. – 9:30 a.m.

Professor Ben Zhong Tang, South China University of Technology

Visualization and Manipulation of Molecular Motion in Solid State by AIEgens

9:30 a.m. – 10:00 a.m.

Professor Jianfang Wang, Chinese University of Hong Kong

Colloidal Plasmonic Metal Nanocrystals

10:00 a.m. – 10:30 a.m.

Coffee Break

10:30 a.m. – 11:00 a.m.

Professor Chun Sing Lee, City University of Hong Kong

Biomedical Applications of Organic Fluorescent and Photovoltaic Materials

11:00 a.m. – 11:30 a.m.

Professor Andrey Rogach, City University of Hong Kong

Shape and Morphology Control of Perovskite Nanocrystals

11:30 a.m. -12:00 a.m.

Professor He Yan, Hong Kong University of Science and Technology

Achieving Non-fullerene Organic Solar Cells with Over 16% Efficiency: Material Design, Device Optimization and Mechanism Study

To register for this free event, please fill out the form below.

 

Thursday, May 16, South China University of Technology

Hosted by: Professor Ben Zhong Tang, South China University of Technology

Agenda:

8:15 a.m. – 8:45 a.m.

Registration

8:45 a.m. – 9:00 a.m.

Professor Bin Liu, ACS Materials Letters Deputy Editor, National University of Singapore

Opening Remarks & Presentation on ACS Materials Letters

9:00 a.m. – 9:30 a.m.

Professor Fei Huang, South China University of Technology

Materials and Devices towards High Efficiency Thick-Film Polymer Solar Cells

9:30 a.m. – 10:00 a.m.

Professor Dan Li, Jinan University

Chemopallet‒A Strategy for Tuning Photoluminescence of Supramolecular Coordination Entities

10:00 a.m. – 10:30 a.m.

Coffee Break

10:30 a.m. – 11:00 a.m.

Professor Zhenguo Chi, Sun Yat-Sen University

Recent Advances in Organic Mechano-Responsive AIE Luminogens

11:00 a.m. – 11:30 a.m.

Professor Shuizhu Wu, South China University of Technology

Photophysical Systems for Detection and Bioimaging

11:30 a.m. – 12:00 p.m.

Professor Zujin Zhao, South China University of Technology

Aggregation-induced Emission Materials for High-performance Non-doped OLEDs

To register for this free event, please fill out the form below.

Friday, May 17, Peking University

Hosted by: Professor Jian Pei, Peking University

Agenda:

1:30 p.m. – 2:00 p.m.

Registration

2:00 p.m. – 2:15 p.m.

Professor Bin Liu, ACS Materials Letters Deputy Editor, National University of Singapore

Opening Remarks & Presentation on ACS Materials Letters

2:15 p.m. – 2:45 p.m.

Professor Xiaowei Zhan, Peking University

ITIC Family Fused-Ring Electron Acceptors for Organic Photovoltaics

2:45 p.m. – 3:15 p.m.

Professor Lin Guo, Beihang University

Synthesis and Properties of Amorphous Nanomaterials

3:15 p.m. – 3:45 p.m.

Coffee Break

3:45 p.m. – 4:15 p.m.

Professor Jin Zhang, Peking University

CVD Growth of Single-walled Carbon Nanotubes with Controlled Structure

4:15 p.m. – 4:45 p.m.

Professor Shu Wang, Institute of Chemistry, Chinese Academy of Sciences

Conjugated Polymer-Based Assembly Materials for Biomedical Applications

4:45 p.m. – 5:15 p.m.

Professor Zhaohui Wang, Tsinghua University

Nano-Carbon Imides: Precise Synthesis and Applications

To register for this free event, please fill out the form below.

Wednesday, May 22, University of Science and Technology of China

Hosted by: Professor Shu-Hong Yu, University of Science and Technology of China

Agenda:

8:15 a.m. – 8:45 a.m.

Registration

8:45 a.m. – 9:00 a.m.

Professor Bin Liu, ACS Materials Letters Deputy Editor, National University of Singapore

Opening Remarks & Presentation on ACS Materials Letters

9:00 a.m. – 9:30 a.m.

Professor Zhiyong Tang, National Center for Nanoscience and Nanotechnology

Self-assembled Supraparticles for Catalytic Application

9:30 a.m. – 10:00 a.m.

Professor Xun Wang, Tsinghua University

Sub-1 nm Ultrathin Nanocrystals

10:00 a.m. – 10:30 a.m.

Coffee Break

10:30 a.m. – 11:00 a.m.

Professor Dan Wang, National Center for Nanoscience and Nanotechnology

Hollow Multi-shelled Structure: Synthesis Chemistry and Applications

11:00 a.m. – 11:30 a.m.

Professor Qiangbin Wang, Suzhou Institute of Nano-tech and Nano-bionics (SINANO)

Advanced In Vivo Fluorescence Imaging: Seeing is Believing

11:30 a.m. – 12:00 p.m.

Professor Hua Zhang, City University of Hong Kong

Phase Engineering of Novel Nanomaterials

To register for this free event, please fill out the form below.

Thursday, May 23, Zhejiang University

Hosted by: Professor Feihe Huang, Zhejiang University

Co-hosted by: Professor Guping Tang, Zhejiang University

Agenda:

8:15 a.m. – 8:45 a.m.

Registration

8:45 a.m. – 9:00 a.m.

Professor Bin Liu, ACS Materials Letters Deputy Editor, National University of Singapore

Opening Remarks & Presentation on ACS Materials Letters

9:00 a.m. – 9:30 a.m.

Professor Feihe Huang, Zhejiang University

Nonporous Adaptive Crystals for Separation of Important Chemicals in Chemical Industry

9:30 a.m. – 10:00 a.m.

Professor Leyong Wang, Nanjing University

The Orthogonal Self-assembly of Supramolecular Materials for Smart Windows

10:00 a.m. – 10:30 a.m.

Professor Chao Gao, Zhejiang University

Macro-assembled Graphene Materials

10:30 a.m. – 11:00 a.m.

Coffee Break

11:00 a.m. – 11:30 a.m.

Professor Yizheng Jin, Zhejiang University

Toward High-performance Light-emitting Diodes Based on Quantum Dots

11:30 a.m. – 12:00 p.m.

Professor Yuan Ping, Zhejiang University

Delivery Materials for Therapeutic Genome Editing

12:00 p.m. – 12:30 p.m.

Professor Yingying Lu, Zhejiang University

Rational Design of Electrode Geometry and Solid Electrolyte Interface for Stable Lithium Metal Anode

To register for this free event, please fill out the form below.

Friday, May 24, Shanghai Jiao Tong University

Hosted by: Professor Chunhai Fan, Shanghai Jiao Tong University

Co-hosted by: Professor Yongfeng Zhou, Shanghai Jiao Tong University

Agenda:

8:15 a.m. – 8:45 a.m.

Registration

8:45 a.m. – 9:00 a.m.

Professor Bin Liu, ACS Materials Letters Deputy Editor, National University of Singapore

Opening Remarks & Presentation on ACS Materials Letters

9:00 a.m. – 9:30 a.m.

Professor Yongfang Li, Institute of Chemistry, Chinese Academy of Sciences

Recent Research Progress of Photovoltaic Materials for Polymer Solar Cells

9:30 a.m. – 10:00 a.m.

Professor Yunqi Liu, Institute of Chemistry, Chinese Academy of Sciences

Polymer Semiconductors with High Carrier Mobility and Their Device Applications

10:00 a.m. – 10:30 a.m.

Coffee Break

10:30 a.m. – 11:00 a.m.

Professor Weihong Tan, Hunan University/Shanghai Jiao Tong University/University of Florida

Molecular Elements: Building Functional Materials Using Nucleic Acids

11:00 a.m. – 11:30 a.m.

Professor He Tian, East China University of Science and Technology

Molecular Dynamic Assembly & Assembling-induced Emissions

11:30 a.m. – 12:00 p.m.

Professor Yang Tian, East China Normal University

Developing New Tools for Understanding the Processes of Oxidative Stress in the Brain

To register for this free event, please fill out the form below.

 

 

ACS Infectious Diseases Young Investigator Award Winners Announced

The ACS Infectious Diseases Young Investigator Award recognizes outstanding young investigators in the infectious diseases field who are within 10 years of their last training experience or at the Assistant Professor level. The 2019 ACS Infectious Diseases Young Investigator  awardees are:

  • Steve D. Townsend, Assistant Professor at Vanderbilt University
  • Jarrod French, Associate Professor at Stonybrook University
  • Megan Wright, University Academic Fellow at the University of Leeds.

The award is jointly presented by ACS Infectious Diseases and the ACS Division of Biological Chemistry.

As winners of the 2019 ACS Infectious Diseases Young Investigator Awards, Townsend, Wright, and French will each receive a plaque, an award of $1,000, and up to $500 in travel reimbursement to attend the Fall 2019 ACS National Meeting & Exposition in San Diego and present at an ACS Division of Biological Chemistry symposium in their honor.

I got the chance to chat with the award winners; read on to find out more about them:

Steve Townsend

How did you get into your field of study?

My primary interest and training are in synthetic organic chemistry. However, as a postdoc, I took an interest in maternal and child health. My goal over the past several years has been to leverage organic chemistry to make discoveries that would translate to reducing the burden of adverse pregnancy outcomes and improve the lives of women and children.

What is the most exciting discovery you have made in your career so far?

Our first big discovery was that human milk oligosaccharides (HMOs) possess potent antimicrobial and antibiofilm activity. The most exciting discovery, however, was that different mothers were producing HMOs with varying levels of potency.

What are you looking forward to most about your research?

The lab currently has two research focuses: Human milk glycoscience and small-molecule total synthesis. Regarding the milk program, I am most excited about deciphering novel interacting partners (perhaps proteins) that milk glycans might engage to provide protection against bacterial pathogens. In our small molecule program, we have recently completed the total synthesis of two natural products. Two others are close!  Therefore, it is an exciting time in the lab as we are displaying our synthetic chops and beginning to study the biology of several interesting molecules. Equal to my excitement about our research results is watching the continued growth of the graduate students in our lab who have entrusted me with helping them develop into independent researchers. Ultimately, I believe that their development, success, and well-being will be my greatest legacy.

Jarrod French

How did you get into your field of study?

Shortly after I started my independent career at Stony Brook in 2014, a colleague approached me from the department of molecular genetics and microbiology. His group works on host-pathogen interactions and the regulation of the immune response. They had recently discovered this exciting phenotype when studying a new class of phosphatase called the Suppressor of TCR Signaling (Sts). A Sts-knockout mouse model strain that they had generated displayed a profound level of resistance to infection by a number of pathogenic organisms. This result suggested that if you could down-regulate the activity of the Sts enzymes in a clinical setting, then you could potentially stimulate the immune response, enhancing the clearance of pathogens and improving outcomes for systemic infections. My colleague and I began to work together, first to characterize the structure and function of this class of protein, and then to search for inhibitors that could act as a basis for drug development. We have been collaborating on this project now for several years and have made tremendous progress, both in our understanding of how this interesting class of protein works and towards the identification of specific inhibitors.

What is the most exciting discovery you have made in your career so far?

I have been fortunate to be involved with a lot of great science over the years. I am proud of all of the work that my lab has done. However, one of the most exciting and rewarding elements of our work is getting to solve a new crystal structure of a protein. Even after dozens of structures, I still get super excited when we solve a new one. To me, it is akin to an explorer discovering a new world. You get to be the first person ever to lay eyes upon this particular arrangement of molecules. It is exciting to be a part of this process, and every new protein structure reveals critical details about function. On top of that, the excitement only just begins there. A new structure of a protein is a jumping-off point – the beginning of many new lines of inquiry.

What are you looking forward to most about your research?

What motivated me to become a scientist in the first place was a real desire to make discoveries and develop new drugs that could one day help to cure disease and save lives. In the beginning, however, I had no idea how difficult, time-consuming and expensive the drug discovery process really is. In spite of that, my group is finally at the point where we have characterized a great drug target, developed assays, completed screens and identified our first few inhibitors. While it may be many years down the road, what I really look forward to most is the opportunity that we may one-day start clinical trials on a compound that we developed. The best possible outcome would be the development of a new immunostimulatory treatment for infectious disease that could be used to save thousands of lives each year.

Megan Wright

How did you get into your field of study?

I did a degree in natural sciences, majoring in chemistry because I loved the creativity and analytical nature of this subject. However, I always had half an eye on biology, and during my degree I did a summer project in the lab of David Spring (University of Cambridge, UK), synthesizing potential inhibitors of bacterial quorum sensing. In the last two weeks of this project, I tested my compounds in a microbiology lab – and from then on, I was hooked on chemical biology! I did a Ph.D. with Ed Tate at Imperial College London developing a chemical approach to identifying lipidated proteins, in collaboration with parasitologists working on different protozoa. This completely opened my eyes to these fascinating organisms and to what you can accomplish working in collaborative teams across disciplines. Then when I was writing postdoctoral fellowship proposals to work with Stephan Sieber (TU Munich) I took inspiration from my initial summer experience to delve back into microbiology. There is something about using chemistry to identify interactions in their native environment — to unravel the inner workings of cells and communication between cells — that really captures my imagination.

What’s the most exciting discovery you’ve made in your career so far?

I find it fascinating that we as chemists can design a tool that closely mimics a molecule yet contains functionality that allows us to understand the fate and interactions of that molecule in a living system. For example, during my postdoctoral fellowship, I wanted to understand how a human peptide triggers virulence in the opportunistic pathogen Pseudomonas aeruginosa. I designed chemical probes based on this peptide to search for the hypothesized bacterial receptor. By combining these probes with proteomics, we discovered a protein sensor that alerts bacteria to the presence of antimicrobial peptides. This is exciting, firstly because no one had shown direct binding of these peptides to proteins in live bacterial cells and so the chemist in me appreciates this technical achievement, but secondly because this sensor seems to be allowing bacteria to mount their defenses in order to thrive in the host. Perhaps this mechanism could be manipulated to help clear bacterial infection? Or maybe these tools will allow us to better understand how Pseudomonas can adapt to different environments? My lab is now developing this chemical approach and applying it to identify other signal-sensor interactions that mediate host-microbe communication.

What are you looking forward to most about your research?

I am most excited about using chemical probes as discovery tools to reveal molecular interactions in live cells and in complex, heterogeneous, cellular systems. I see my lab focusing in two main areas. First, using chemical tools to discover new mechanisms of communication between microbes and their hosts; there must be a huge number of molecules, receptors, and pathways operating in complex multispecies environments that we know nothing about and I think chemical biology can really contribute to this area. Secondly, I want to develop methods that can interrogate dynamic protein function in cells. We are just starting a new project developing probes that can label or trap proteins in specific states in living cells and with spatial and temporal control. This will allow us to start to unravel how cells integrate signals and respond to changing conditions. This is a fundamental biological question, but also one that is central to infectious disease.

The journal and the Division encourage you to attend the ACS Infectious Diseases Young Investigator Awards Symposium at the 2019 ACS National Fall Meeting in San Diego

  • Global Health: Biology and Chemistry of Waterborne Diseases
    • Tuesday, August 27, 8:30 am
    • Marriott Marquis San Diego Marina, Marriott Grand Ballroom Section 6
  • ACS Infectious Diseases Young Investigators Award Symposium
    • Tuesday, August 27, 1:00 pm
    • Marriott Marquis San Diego Marina, Marriott Grand Ballroom Section 6

Professor Heather D. Maynard to Receive the 2019 Bioconjugate Chemistry Lectureship Award

Bioconjugate Chemistry and the ACS Division of Polymeric Materials Science and Engineering are pleased to announce that Professor Heather D. Maynard of the University of California, Los Angeles (UCLA) is the recipient of the 2019 Bioconjugate Chemistry Lectureship Award. The award will be presented at the 2019 ACS Fall National Meeting & Exposition, held August 25 – 29 in San Diego. Maynard will be presenting as part of the Bioconjugate Chemistry Lecturer Symposium at the meeting, along with other prominent researchers in the field.

Heather D. Maynard is the Dr. Myung Ki Hong Professor in Polymer Science in the Department of Chemistry and Biochemistry and the California NanoSystems Institute at UCLA. Maynard is a leader in the area of protein-polymer conjugates, which are important therapeutics for a variety of diseases. She develops new synthetic methods to make the materials, invents new polymers to improve properties such as stability, and demonstrates preclinical efficacy of her conjugates with an eye towards translation for human health. Maynard also works in the area of smart materials for precision medicine: materials that respond to disease states in the body.

Maynard’s research and teaching have been recognized by numerous awards, including most recently the Bioconjugate Chemistry Lectureship Award, the American Chemical Society Arthur Cope Scholar Award, the UCLA Student Development Diversity, Equity and Inclusion Award, and election as an American Association for the Advancement of Science (AAAS) Fellow. Maynard is also an American Chemical Society POLY and PMSE, Leverhulme, Kavli Frontiers, and Royal Society of Chemistry Fellow, was a Fulbright Specialist in New Zealand, and a member of the US Defence Science Study Group.  Maynard received her PhD from the California Institute of Technology and was an American Cancer Society Postdoctoral fellow at the Swiss Federal Institute of Technology (ETH).

“Heather Maynard’s creativity  has generated truly amazing new science at the interface between the biological and chemical world,” said Bioconjugate Chemistry Editor-in-Chief, Vincent M. Rotello.

Read a Selection of Professor Heather D. Maynard’s Research:

PEG Analogs Synthesized by Ring-Opening Metathesis Polymerization for Reversible Bioconjugation
Bioconjugate Chem., 2018, 29 (11), pp 3739–3745
DOI: 10.1021/acs.bioconjchem.8b00635

Trehalose Glycopolymer Enhances Both Solution Stability and Pharmacokinetics of a Therapeutic Protein
Bioconjugate Chem., 2017, 28 (3), pp 836–845
DOI: 10.1021/acs.bioconjchem.6b00659

Protein–Polymer Conjugation via Ligand Affinity and Photoactivation of Glutathione S-Transferase
Bioconjugate Chem., 2014, 25 (10), pp 1902–1909
DOI: 10.1021/bc500380r

Check back as this post is updated with details about the 2019 ACS Fall National Meeting Bioconjugate Chemistry Lecturer Symposium!