Shuguang Zhang

Research Affiliate
  • Molecular Machines

Learn more about Shuguang Zhang's research at the Molecular Architecture website.

Shuguang Zhang is at the MIT Media Lab. He received his BS from Sichuan University, China and PhD in biochemistry and molecular biology from the University of California at Santa Barbara, USA. He was an American Cancer Society Postdoctoral Fellow, a Guggenheim Fellow, and a Whitaker Foundation Investigator at MIT. He was a 2003 fellow of Japan Society for Promotion of Science (JSPS fellow). His work of designer self-assembling peptide scaffold won 2004 R&D100 award. He won the 2006 Wilhelm Exner Medal of Austria. He was elected to American Institute of Medical and Biological Engineering in 2011 and elected to US National Academy of Inventors in 2013. He was elected to Austrian Academy of Sciences in 2010 and  European Academy of Sciences and Arts in 2021. He won the 2020 Emil Thomas Kaiser Award from the Protein Society.   He is a  honorary member of the Schrödinger Society and was  invited to deliver a lecture at the 20th Erwin Schrödinger Colloquium, by the Schrödinger Society at the Austrian Academy Sciences in Vienna,  Austria on December 17,  2021.  He is the recipient of the Eva and George Klein Medal and delivered the George Klein Lecture at the Karolinska Institute, Stockholm, Sweden in April 2024. 

He has published over 200 scientific papers that have so far been cited over 39,900 times and with an h-index of 96. He is also a co-founder and board member of the Molecular Frontiers Foundation that encourages young people to ask the best questions in order to win the Molecular Frontiers Inquiry Prize.

Shuguang Zhang made a serendipitous discovery of a repetitious and ionic self-complementary peptide segment in yeast protein Zuotin in 1990. This is the discovery of the first self-assembling peptides that eventually led to the development of a new field of peptide nanobiotecnology. Furthermore, his discovery inspired numerous people around the world to design a variety of self-assembling peptides for widespread uses including peptide hydrogels in materials science, 3D tissue cell culture, 3D tissue printing and tissue engineering, nanomedicine, sustained molecular releases, clinical and surgical applications. He co-founded a startup company that has made significant contributions to bring the self-assembling peptide materials to human clinical and surgical use. He founded a biotech company 3-D Matrix in 2002 that went to IPO in October 2011. It had a US$1 billion market capitalization in 2013.

Shuguang Zhang in 2011 conceived and invented a simple molecular QTY Code to design proteins, particularly membrane proteins, and perhaps other aggregated proteins. Not only do these engineered membrane receptor proteins become water-soluble with little changing molecular weight and pI, but these detergent-free (water-soluble) membrane proteins also retain their biological function, namely bind their natural ligands.  With his colleagues, they recently showed that QTY code also applied to engineer membrane protein enzyme  histidine kinase into the water-soluble form.  Histidine kinase not only retains its structure, but also its 4 separate  enzyme functions.  The water-soluble histidine kinase enzyme can be a target for discovering new class of antibiotics.  His invention of the QTY Code technology will likely have a big impact in engineering a variety of membrane proteins and perhaps some water-insoluble and aggregated proteins. He is a co-founder of a biotech company OH2 Laboratories and 511 Therapeutics that will commercialise the technology. It will likely transform many aspects of drug discovery and new therapies.

Furthermore, recently during large gene library synthesis and due to an imperfect DNA assembly (a technical mistake), he made an unexpected discovery in 2014 that some non-full-length membrane receptors can still bind their natural ligands. This discovery has far reaching implications for the so-called pseudo-genes in genomes. Some of such pseudo-genes may code for non-full-length proteins that may still be involved in biological regulations. Similar to microRNA, this discovery may alert scientists to carefully study the overlooked widespread pseudo-genes in genomes.