title: Serine protease inhibitor mediated peptide bond re-synthesis in diverse protein molecules.
abstract: Protease inhibitors have been extensively used in research to prevent unwanted degradation of proteins during purification and analysis. Here, we report a remarkable discovery of protease inhibitor mediated reformation of peptide bonds by the serine protease inhibitor, PMSF in a diverse set of proteolyzed molecules. Interestingly, the religation reaction in the presence of PMSF occurs in a very short time period and with very high yields of the religated product. We also investigate the plausible mechanism of such a reaction and demonstrate through biochemical studies and X-ray crystallography that proximity of reacting termini is essential for the feasibility of this reaction.
authors: Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036, India.
authors: Amit
authors: A
authors: Sharma
authors: K V
authors: KV
authors: Radha Kishan
mesh_terms: D000818:Animals; D008958:Models, Molecular; D009113:Muramidase / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D059748:Proteolysis / Q000187:drug effects; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D013381:Subtilisins / Q000037:antagonists & inhibitors* / Q000378:metabolism
chemical_list: D010455:Peptides; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D010664:Phenylmethylsulfonyl Fluoride; D009113:Muramidase; D013381:Subtilisins