Screening a Peptide Library by DSC and SAXD: Comparison with the Biological Function of the Parent Proteins
Author(s) -
Ana J. Pérez-Berná,
Georg Pabst,
Peter Laggner,
José Villalaı́n
Publication year - 2009
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0004356
Subject(s) - peptide , peptide library , membrane protein , function (biology) , biology , computational biology , integral membrane protein , lipid bilayer fusion , chemistry , biochemistry , biophysics , membrane , microbiology and biotechnology , peptide sequence , gene
We have recently identified the membranotropic regions of the hepatitis C virus proteins E1 , E2 , core and p7 proteins by observing the effect of protein-derived peptide libraries on model membrane integrity. We have studied in this work the ability of selected sequences of these proteins to modulate the L β -L α and L α -H II phospholipid phase transitions as well as check the viability of using both DSC and SAXD to screen a protein-derived peptide library. We demonstrate that it is feasible to screen a library of peptides corresponding to one or several proteins by both SAXD and DSC. This methodological combination should allow the identification of essential regions of membrane-interacting proteins which might be implicated in the molecular mechanism of membrane fusion and/or budding.
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