Shuguang Zhang received his B.S. in biochemistry from Sichuan University in 1980 and Ph.D. in Biochemistry & Molecular Biology from University of California at Santa Barbara in 1988 (under mentorship of Eduardo Orias). The same year, he joined MIT to work with Alexander Rich.

Self-Assembling Peptides edit

In 1990, Shuguang Zhang made a serendipitous discovery of a self-assembling peptide in yeast protein Zuotin.^[8][9] This discovery led to the development of a new field of peptide nanobiotechnology and to designs of a variety of self-assembling peptides for widespread uses, including peptide hydrogels in materials science, 3D tissue cell culture and tissue engineering, nanomedicine, sustained molecular releases, clinical and surgical applications.^{[10][11][12][13]} He co-founded a startup company 3DMatrix that brings the self-assembling peptide materials to human clinical for treatment of diabetic ulcers, bedsores (pressure ulcers) and for accelerated wound healings as well as surgical uses.^[14] Many self-assembling peptide scaffold hydrogel products have received approvals from the US FDA, European Medicine Agency (EMA), Japan Medical Agency and medical approval agency in Chengdu, China.^[15]

QTY Code edit

Less widely-known, Zhang invented the QTY Code as a systematic method of rendering insoluble peptide sequences water-soluble, to facilitate biochemical research, while retaining the native conformation and functionality.^{[16][17][18][19]} In 2011, Shuguang Zhang started to design membrane proteins, because there are ~26% of genes that code for membrane proteins in genomes which are crucial for both internal and external cellular communications.^[20][21] He conceived a simple molecular QTY Code, namely Glutamine (Q), Threonine (T) and Tyrosine (Y) to systematically replace the hydrophobic amino acids Leucine (L), Valine (V), Isoleucine (I), and Phenylalanine (F) in the 7 transmembrane alpha-helices of G protein-coupled receptors (GPCRs).^[16][18] Thus, it changes the water-insoluble form of membrane proteins, including GPCRs, into a water-soluble form. The QTY code results suggest that despite 46%-56% transmembrane alpha-helices changes, water-soluble QTY variants still maintain stable structures and biological function, namely, ligand-binding activities. This simple QTY code is a likely useful tool and has big impact for designs of water-soluble variants of previously water-insoluble and perhaps aggregated proteins, including amyloids.^[16]

• American Cancer Society Postdoctoral Fellow
• Whitaker Foundation Investigator, MIT
• 2006 Guggenheim Fellowship^[22]
• Academic sabbatical at University of Cambridge^[23]
• 2006 Wilhelm Exner Medal of Austria^[24]
• Elected to Austrian Academy of Sciences, 2010^[25]
• Elected to American Institute of Medical and Biological Engineering, 2011^[26]
• Elected to US National Academy of Inventors, 2013^[27]
• 2020 Emil Thomas Kaiser Award from the Protein Society^[28]
• Elected to European Academy of Science and Arts, 2021^[29]
• Elected honorary fellow, Erwin Schrödinger Society at the Austrian Academy of Sciences, 2021^[30]