1. Mechanism of Biologcial Molecules Explored via NMR spectroscopy in Solution and Its Native Enviorments

Chaperones are crucial for cellular life to ensure all proteins obtain their right fold and functionality. The promiscuous property of chaperones enables them to bind with a wide spectrum of client proteins from nascent proteins to quasi-native and native proteins. While mechanisms of chaperones aided protein folding have been intensively characterized, it is still largely unknown how chaperones act on folded clients and modulate the activity of the folded protein. To address this fundamental question, We apply NMR spectroscopy and other biophysics approaches to understand chaperone and client proteins recognition and interaction by investigating their intermediate conformations (excited state), protein dynamics modulations and the subsequently changes of its activities. 

2. Mechanism of Bacteria Alter Host Innate Immune Response via Outer Membrane Vesicles(OMVs)

Bacterial outer membrane vesicles (OMVs) are nano‐sized compartments consisting of a lipid bilayer that encapsulates periplasm‐derived, luminal content. OMVs, which pinch off of Gram‐negative bacteria, are now recognized as a generalized secretion pathway which provides a means to transfer cargo to other bacterial cells as well as eukaryotic cells. Although it is well recognized that OMVs can enter and release cargo inside host cells during infection, the mechanisms of host association and uptake are not well understood. We apply biophysical, biochemical and cellular biological approaches to investigate characters of virulence factors in OMVs and study the mechanism of host cell association, uptake and innate immunue response to OMVs.

3. Mechanism of Transmembrane Domain in Signaling Transduction

We applied NMR to investigate the structural and functional roles of the transmembrane and membrane-proximal regions of cell surface proteins with special focus on CAR-T transmembrane domain, innate immune response receptors and viral proteins.

4. Nanobody Screening and Epitope Mapping via NMR

Single-domain antibody, also known as a nanobody, is an antibody fragment from Camelid consisting of a single monomeric variable antibody domain. It has a molecular weight of only 12–15 kDa. Nevertheless it is able to bind with a particular antigen with a high affinity. Besides higher affinity, smaller size, nanobody also has other advantages such as higher stability and easy expression in E.coli facilitating isotope labeling and epitope mapping via NMR.

Editorship & Membership

2021-09， Cell Press: The Innovation， Youth Editor

2021-07, LIFE,  Special Issue Editor

2021-08, BIOMOLECULES,  Topical Advisory Panel Membership

          Bin Yu                 Yun Peng              Mengyi Wu             Yaling Zhao

         Postdoc                 Postdoc               Technician               Technician

University of Basel, Switzerland

Friedrich-Loeffler-Institut, Germany

     Guan Wang         Yihao Chen            Shixing Qi                Zhiqing Tao        Mingjun Zhu       Ruishen Ding

   Graudate Student      Graudate Student         Graudate Student            Graudate Student      Graudate Student     Graudate Student

ChaoZhe Wang       Huan Wang

 Graudate Student       Graudate Student 

Yangzhuoyue Jin           Yilin Zhuo            Jie  Yang                     Yun Xia                   Junli Long

  Undergraduate       Undergraduate     Undergraduate           Undergraduate          Undergraduate

（1） Expression, purification, refolding, and characterization of octreotide-interleukin-2: a chimeric tumor-targeting protein, Int J Mol Med., 2011

（2） Solid-state NMR resonance assignments of the filament-forming CARD domain of the innate immunity signaling protein MAVS, Biomol NMR Assign., 2014

（3） Structure determination of helical filaments by solid-state NMR spectroscopy, Proc Natl Acad Sci U S A., 2016

（4） A molecular mechanism of chaperone-client recognition., Science Advances, 2016

（5） Therapeutic silence of pleiotrophin by targeted delivery of siRNA and its effect on the inhibition of tumor growth and metastasis, PLoS One, 2017

（6） An unexpected protective role of low affinity allergen-specific IgG via the inhibitory receptor FcrRIIb, J. Allergy Clin. Immunol., 2017, 

（7） Common Patterns in Chaperone Interactions with a Native Client Protein., Angew.Chemie Int. Ed., 2018,

（8） Frustrated Interfaces Facilitate Dynamic Interactions between Native Client Proteins and Holdase Chaperones, ChembioChem, 2019-06

From 2019

（1） Mechanisms of Chaperones as Active Assistant/Protector for Proteins: Insights from NMR Studies, Chinese Journal of Chemistry, 2019-12

（2） NMR-Based Methods for Protein Analysis， Anal Chem.， 2020

（3） Cellular stress promotes NOD1/2-dependent inflammation via the endogenous metabolite sphingosine-1-phosphate， The EMBO Journal, 2021 

（4） Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation， mBio， 2021

（5） Backbone resonance assignments and dynamics of S. cerevisiae SERF,  Biomolecular NMR Assignments, 2022

（6） Molecular Insight into the Extracellular Chaperone Serum Albumin in Modifying the Folding Free Energy Landscape of Client Proteins，Journal of Physical Chemistry Letters， 2022

（7） Self-Assembled Oligopeptide (FK)4 as a Chiral Alignment Medium for the Anisotropic NMR Analysis of Organic Compounds，ACS Applied Materials & Interfaces， 2022 

Contact:

Prof. Dr. Lichun He 

Wuhan Institute of Physics and Mathematics, CAS

Add:West No.30 Xiao Hong Shan,Wuhan 430071 China

Tel:+86-27-87197309

Email: helichun@apm.ac.cn

Join Us:

We are looking for highly motivated International Ph.D Student and Postdoc. Please contact helichun@apm.ac.cn