Self-Assembling Peptides
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
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]
