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Serine protease inhibitor mediated peptide bond re‐synthesis in diverse protein molecules
Author(s) -
Sharma Amit,
Radha Kishan K.V.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.10.004
Subject(s) - pmsf , serine protease , protease , chemistry , peptide , proteases , serine , protease inhibitor (pharmacology) , biochemistry , peptide bond , stereochemistry , enzyme , biology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , immunology
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.