Shuguang Zhang

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 33,000 times with an h-index of 85.[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.

Shuguang Zhang
Born
Chongqing, China
Known forself-assembling peptides
Academic background
EducationUniversity of California, Santa Barbara (Ph.D.), Sichuan University (B.S.)
Doctoral advisorEduardo Orias
Academic work
DisciplineBiochemistry
Sub-disciplineMolecular Architecture
InstitutionsMassachusetts Institute of Technology
Websitehttps://www.media.mit.edu/people/shuguang/overview/

Early life and education

Shuguang Zhang received his B.S. in biochemistry from the Sichuan University in Chengdu, China in 1980. In 1988 he received his Ph.D. in Biochemistry & Molecular Biology from the University of California, Santa Barbara (UCSB). He joined the Massachusetts Institute of Technology in 1988 to work with Alexander Rich.

Career and Scientific Work

Self-Assembling Peptides

Zhang is widely acknowledged as the founder of the field of self-assembling peptide materials.[5][6][7] His discovery in Alexander Rich’s laboratory that the yeast protein Zuotin[8] spontaneously self-assembles to form a macroscopic membrane[9] inspired researchers to develop new biomimetic peptide materials [10] with applications in biological research and therapeutics[11][12]

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.[13][14][15][16]

References
  1. "Shuguang Zhang, MIT Media Lab, People". MIT Media Lab.
  2. "Shuguang Zhang". scholar.google.com.
  3. "ORCiD Shuguang Zhang".
  4. Baas, Jeroen (2020). "Bibliometrics". Mendeley Data. 2. Mendeley. doi:10.17632/btchxktzyw.2.
  5. "The Protein Society 2020 Award Recipients".
  6. Zhang, Shuguang (October 20, 2017). "Discovery and design of self-assembling peptides". The Royal Society Interface Focus. 7 (6): 20170028. doi:10.1098/rsfs.2017.0028. PMC 5665798. PMID 29147558.
  7. "The Foundation for Regenerative Medicine - Self-Assembling Peptides".
  8. Zhang, Shuguang (October 11, 1992). "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae". The EMBO Journal. 11 (10): 3787–3796. doi:10.1002/j.1460-2075.1992.tb05464.x. PMC 556839. PMID 1396572.
  9. Zhang, S (April 15, 1993). "Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane". Proc. Natl. Acad. Sci. USA. 90 (8): 3334–3338. Bibcode:1993PNAS...90.3334Z. doi:10.1073/pnas.90.8.3334. PMC 46294. PMID 7682699.
  10. Levin, Aviad (September 15, 2020). "Biomimetic peptide self-assembly for functional materials". Nature Reviews Chemistry. 4 (11): 615–634. doi:10.1038/s41570-020-0215-y. S2CID 221718855.
  11. Gelain, Fabrizio (February 17, 2021). "Self-assembling peptide scaffolds in the clinic". NPJ Regenerative Medicine. 6 (1): 9. doi:10.1038/s41536-020-00116-w. PMC 7889856. PMID 33597509.
  12. Yang, Jia (2021). "Self-Assembled Peptide Drug Delivery Systems". ACS Appl. Bio. Mater. 4: 24–46. doi:10.1021/acsabm.0c00707. S2CID 225639201.
  13. Zhang, Shuguang (September 11, 2018). "QTY code enables design of detergent-free chemokine receptors that retain ligand-binding activities". Proc. Natl. Acad. Sci. USA. 115 (37): E8652–E8659. doi:10.1073/pnas.1811031115. PMC 6140526. PMID 30154163.
  14. Qing, Rui (December 17, 2019). "QTY code designed thermostable and water-soluble chimeric chemokine receptors with tunable ligand affinity". Proc. Natl. Acad. Sci. USA. 116 (51): 25668–25676. doi:10.1073/pnas.1909026116. PMC 6926000. PMID 31776256.
  15. Arnaud, Celia (August 29, 2018). "Following a code for swapping amino acids makes membrane proteins water soluble". Chemical & Engineering News. 96.
  16. Trafton, Anne (August 28, 2018). "Scientists alter membrane proteins to make them easier to study". Phys.org.
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