Development and application of serine/threonine ligation for synthetic protein chemistry.
Chemical synthesis of proteins, especially those with post-translational modifications, has offered new opportunities to study the protein structure-function relationship. In the past four years, we have developed the serine/threonine ligation (STL), which involves the chemoselective reaction between peptide salicylaldehyde esters and peptides with N-terminal serine or threonine. The method has been successfully applied to the synthesis of both linear and cyclic peptides/proteins.
Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, P. R. China. xuechenl@hku.hk.
Han
H
Liu
Xuechen
X
Li
D017766:Acid Anhydride Hydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D060326:Chemistry Techniques, Synthetic / Q000379:methods*; D004912:Erythrocytes / Q000201:enzymology; D004952:Esters / Q000737:chemistry; D008969:Molecular Sequence Data; D018396:Mucin-1 / Q000378:metabolism; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry; D012694:Serine / Q000138:chemical synthesis* / Q000737:chemistry; D013912:Threonine / Q000138:chemical synthesis* / Q000737:chemistry; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D004952:Esters; D018396:Mucin-1; D010456:Peptides, Cyclic; D012694:Serine; D013912:Threonine; D000097024:Acylphosphatase