Louis D, Bernillon J, Païsse J O, Wallach J M
Laboratoire de Biochimie Analytique et de Synthèse Bioorganique, Université Claude Bernard-Lyon 1, Villeurbanne, France.
J Chromatogr B Biomed Sci Appl. 1999 Sep 24;732(2):271-6. doi: 10.1016/s0378-4347(99)00301-1.
The use of a peptide library of limited size, is considered to be more appropriate for studying a protease with a complex specificity, but very sensitive 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 serralysin specificity. All compounds of the peptide library could be identified by a LC-MS procedure. After hydrolysis of the library by pseudomonal serralysin, the LC-MS procedure also allowed the identification of the hydrolysis products and the different cleavage sites of the substrates.
