Shuguang Zhang is an American biochemist. He is at the MIT Media Lab's Laboratory for Molecular Architecture.[1] Shuguang Zhang's research focuses on designs of biological molecules, particularly proteins and peptides. He has published over 170 scientific papers, which have cumulatively been cited over 35,000 times with an h-index of 88.[2][3] On the “Updated science-wide author databases of standardizes citation indicators”,[4] he is ranked 18th worldwide in the field of Biomedical Engineering.
Zhang is also a co-founder and board member of Molecular Frontiers Foundation,[5] which organizes annual Molecular Frontiers Symposia in Sweden and around the world.[6] The selected winners are awarded Molecular Frontiers Inquiry Prize.[7]
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]
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]
