Use of liquid chromatography-mass spectrometry coupling for monitoring the serralysin-catalyzed hydrolysis of a peptide library.
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.
Louis
D
D
Laboratoire de Biochimie Analytique et de Synthèse Bioorganique, Université Claude Bernard-Lyon 1, Villeurbanne, France.
Bernillon
J
J
Païsse
J O
JO
Wallach
J M
JM
D002384:Catalysis; D002853:Chromatography, Liquid / Q000379:methods*; D015195:Drug Design; D016903:Drug Monitoring; D006868:Hydrolysis; D013058:Mass Spectrometry / Q000379:methods*; D008666:Metalloendopeptidases / Q000378:metabolism*; D010452:Peptide Biosynthesis; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology
D019151:Peptide Library; D010455:Peptides; D008666:Metalloendopeptidases; C095666:serralysin