Junfeng Zhao
Professor
Guangzhou Medical University
Talk Information
Sustainability in Peptide Science
17 June 2025, 08:30am - 08:45am, in the Pacific Jewel Ballroom
L23 – Peptide Synthesis Using Unprotected Amino Acids
Professor Junfeng Zhao is a faculty member at Guangzhou Medical University, where he leads research in synthetic organic chemistry and chemical biology. His work focuses on developing novel methodologies for peptide and protein modification, with applications in drug discovery and green chemistry.
Academic Background
Dr. Zhao obtained his M.Sc. degree from Central China Normal University in 2005 and completed his Ph.D. at Nanyang Technological University in 2010. He pursued postdoctoral research at Nanyang Technological University, the University of Bonn, and the University of Münster between 2010 and 2013. Subsequently, he served as a Research Assistant Professor at The University of Hong Kong. In 2014, he began his independent academic career as a full professor at Jiangxi Normal University. In 2021, Dr. Zhao and his research group transitioned to Guangzhou Medical University.
Research Focus
Professor Zhao's research centers on the development of innovative synthetic methodologies, particularly in the realm of peptide and protein chemistry. His team has pioneered the use of ynamide coupling reagents to facilitate amide and peptide bond formation with minimal racemization, enabling efficient synthesis of complex biomolecules. This approach has been instrumental in advancing inverse peptide synthesis strategies using unprotected amino acids, contributing to more sustainable and atom-economical peptide production methods.
Notable Contributions
Dr. Zhao has significantly impacted the field of peptide synthesis through his development of ynamide-mediated coupling techniques. His work has been published in reputable journals, including the Journal of the American Chemical Society and Accounts of Chemical Research, highlighting the practical applications of his methodologies in green chemistry and pharmaceutical synthesis. His research offers promising avenues for the efficient and environmentally friendly production of peptide-based therapeutics.
Professional Engagements
Beyond his research endeavors, Professor Zhao actively collaborates with academic institutions and participates in scientific seminars. Notably, he engaged in a joint seminar with the Jiajia Ma Research Group at Shanghai Jiao Tong University, fostering academic exchange and collaboration. His commitment to advancing chemical sciences is evident through his ongoing contributions to both research and the broader scientific community.
Through his innovative research and dedication to sustainable chemical practices, Professor Junfeng Zhao continues to make significant contributions to the fields of synthetic chemistry and chemical biology.
Peptide Synthesis Using Unprotected Amino Acids
School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou, China
The dramatically increased request for peptide active pharmaceutical ingredient (API) stimulates innovations for chemical peptide synthesis. The mandatory use of Nα-protecting group for amino acids in peptide synthesis results in poor step- and atom-economy. At least three steps are required for incorporating each single amino acid, resulting in metric tons of chemical waste for one kilogram of peptide. Sustainable peptide bond formation has been identified as one of the top 10 challenges of green chemistry research area.
Current peptide synthesis relies heavily on legacy technologies and reagents developed before the establishment of green chemistry principles. Only the innovations in peptide synthesis principles can address the poor atom-economic issue fundamentally. Peptide synthesis using unprotected amino acids represents an attractive ideal strategy for greening peptide synthesis because it gets rid of protection and deprotection.
However, C→N peptide elongation is plagued by polymerization while N→C inverse peptide synthesis is retarded by severe epimerization when using unprotected amino acids. Herein, we successfully addressed the notorious epimerization issue of N→C peptide synthesis by employing ynamide coupling reagents. The first practical peptide synthesis by using unprotected amino acids as the building blocks via a transient protection strategy has been accomplished. It is not only effective for solution phase peptide synthesis but also amenable to fragment condensation and solid phase peptide synthesis.
Undoubtedly, this study will spur innovations for using unprotected amino acids and open a new era for peptide synthesis.