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          Institute: MPI für bioanorganische Chemie     Collection: MPI für bioanorganische Chemie     Display Documents



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ID: 712812.0, MPI für bioanorganische Chemie / MPI für bioanorganische Chemie
A caged substrate peptide for matrix metalloproteinases
Authors:Decaneto, Elena; Abbruzzetti, Stefania; Heise, Ingeborg; Lubitz, Wolfgang; Viappiani, Christiano; Knipp, Markus
Language:English
Date of Publication (YYYY-MM-DD):2015
Title of Journal:Photochemical & Photobiological Sciences
Journal Abbrev.:Photochem.Photobiol.Sci.
Volume:14
Issue / Number:2
Start Page:300
End Page:307
Review Status:Internal review
Audience:Experts Only
Abstract / Description:Based on the widely applied fluorogenic peptide FS-6 ( Mca-Lys-Pro-Leu-Gly-Leu-Dpa-Ala-Arg-NH2; Mca = methoxycoumarin-4-acetyl; Dpa = N-3-(2,4-dinitrophenyl)l-alpha,beta-diaminopropionyl) a caged substrate peptide Ac-Lys-Pro-Leu-Gly-Lys*-Lys-Ala-Arg-NH2 (*, position of the cage group) for matrix metalloproteinases was synthesized and characterized. The synthesis implies the modification of a carbamidated lysine side-chain amine with a photocleavable 2-nitrobenzyl group. Mass spectrometry upon UV irradiation demonstrated the complete photolytic cleavage of the protecting group. Time-resolved laser-flash photolysis at 355 nm in combination with transient absorption spectroscopy determined the bi-phasic decomposition with tau(a) = 171 +/- 3 ms (79%) and tau(b) = 2.9 +/- 0.2 ms (21%) at pH 6.0 of the photo induced release of the 2-nitrobenzyl group. The recombinantly expressed catalytic domain of human membrane type I matrix metalloproteinase (MT1-MMP or MMP-14) was used to determine the hydrolysis efficiency of the caged peptide before and after photolysis. It turned out that the cage group sufficiently shields the peptide from peptidase activity, which can be thus controlled by UV light.
Comment of the Author/Creator:Date: 2015, 2015
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für bioanorganische Chemie
External Affiliations:[Abbruzzetti,S.] Univ Parma, Dept Life Sci, I-43124 Parma, Italy.
[Viappiani,C.] Univ Parma, Dept Phys & Earth Sci, I-43124 Parma, Italy.
Identifiers:ISI:000349364700011 [ID No:1]
ISSN:1474-905X [ID No:2]
DOI:10.1039/c4pp00297k [ID No:3]
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