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Title: Analysis of type I signal peptidase affinity and specificity for preprotein substrates
Authors: Geukens, Nick ×
Frederix, F
Reekmans, G
Lammertyn, Elke
Van Mellaert, Lieve
Dehaen, Wim
Maes, Guido
Anné, Jozef #
Issue Date: Jan-2004
Publisher: Academic press inc elsevier science
Series Title: Biochemical and Biophysical Research Communications vol:314 issue:2 pages:459-467
Abstract: Type I signal peptidases (SPases) are membrane-bound endopeptidases responsible for the catalytic cleavage of signal peptides from secretory proteins. Here, we analysed the interaction between a bacterial type I SPase and preprotein substrates using surface plasmon resonance. The use of a home-made biosensor surface based on a mixed self-assembled monolayer of thiols on gold allowed qualitative and kinetic analysis. In vitro binding of purified preproteins to a covalently immobilised bacterial SPase was found to be rather efficient (apparent K-D=10(-7)-10(-8) M). The signal peptide was shown to be a prerequisite for SPase binding and the nature of the mature part of the preprotein significantly affected SPase binding affinity. The developed biosensor containing immobilised SPase is of great importance for analysis of specificity at substrate binding level and for drug screening. In fact, this is the first report of a membrane protein that was covalently attached to a biosensor surface and that retained binding capacity. (C) 2003 Elsevier Inc. All rights reserved.
URI: 
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Bacteriology (Rega Institute)
Molecular Design and Synthesis
Quantum Chemistry and Physical Chemistry Section
Centre for Sociological Research
× corresponding author
# (joint) last author

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