Use of liquid chromatography-mass spectrometry coupling for monitoring theserralysin-catalyzed hydrolysis of a peptide library

The use of a peptide library of limited size, is considered to be more appr opriate for studying a protease with a complex specificity, but very sensit ive and efficient analytical techniques must be used. We have designed and synthesized a 49-peptide library of the type Z-AlaXXAla(amide) (X=Ala, Leu, Val, Phe, Ser, Arg, Glu) for studying the Pseudomonas aeruginosa serralysi n specificity. All compounds of the peptide library could be identified by a LC-MS procedure. After hydrolysis of the library by pseudomonal serralysi n, the LC-MS procedure also allowed the identification of the hydrolysis pr oducts and the different cleavage sites of the substrates. (C) 1999 Elsevie r Science B.V. All rights reserved.