Synthesis of the pro-peptide of subtilisin BPN'
Cash, P.W.; Zhu, X.; Ohta, Y.; Tsao, J.; Lackland, H.; Mateos-Nevado, M.D.; Inouye, M.; Stein, S.; Jordan, F.; Tous, G.I.
Peptide Research 2(4): 292-296
1989
ISSN/ISBN: 1040-5704 PMID: 2520768 Document Number: 340143
Subtilisin, a bacterial serine protease, is secreted as pre-pro-subtilisin. Previously, we demonstrated that the pro-peptide moiety of intact pro-subtilisin can guide the folding of inactive protein to active enzyme both in an intramolecular (6) and intermolecular manner (18). Herein is reported the total chemical synthesis of the pro-sequence (77 amino acids) of pre-pro-subtilisin BPN' carried out by solid phase methods. The structure was confirmed by both sequencing and amino acid analysis of the fragment peptides resulting from a V-8 protease digest. Preliminary studies indicate that the synthetic pro-peptide itself can renature denatured subtilisin BPN'. This study demonstrates a novel method for examining protein folding with the aid of exogenously added synthetic peptides.