A novel method for selection of chymotrypsin inhibitors from a phage peptide library.
A novel screening strategy has been developed for the identification of alpha-chymotrypsin inhibitors from a phage peptide library. In this strategy, the standard affinity selection protocol was modified by adding a proteolytic cleavage period to avoid recovery of alpha-chymotrypsin substrates. After four cycles of selection and further activity assay, a group of related peptides were identified by DNA sequencing. These peptides share a consensus sequence motif as (S/T)RVPR(R/H). Then, a corresponding short peptide (Ac-ASRVPRRG-NH2) was synthesized chemically and proved to be an inhibitor of alpha-chymotrypsin. The present work provides a useful way for searching proteinase inhibitors without detailed knowledge of the molecular structure.
Liu
Y
Y
Department of Molecular Biology, Jilin University, Changchun, P.R. China.
Li
B
B
Zhang
S
S
Li
T
T
Zhou
H
H
Li
W
W
Smith
R
R
de Jersey
J
J
D001435:Bacteriophages / Q000378:metabolism*; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000821:virology; D006868:Hydrolysis; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D019151:Peptide Library; D011485:Protein Binding / Q000187:drug effects; D015202:Protein Engineering / Q000379:methods; D015842:Serine Proteinase Inhibitors / Q000378:metabolism / Q000494:pharmacology*
D009842:Oligopeptides; D019151:Peptide Library; D015842:Serine Proteinase Inhibitors; D002918:Chymotrypsin