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Calmodulin interacts with amphiphilic peptides composed of all D-amino acids

Authors :
Fisher, Phyllis J.
Prendergast, Franklyn G.
Ehrhardt, Mark R.
Urbauer, Jeffrey L.
Wand, A. Joshua
Sedarous, Salah S.
McCormick, Daniel J.
Buckley, Paul
Source :
Nature. April 14, 1994, Vol. 368 Issue 6472, p651, 3 p.
Publication Year :
1994

Abstract

Use of melittin and RS20 that contain only D-amino acids indicates that calmodulin binds avidly to both, revealing the high sterical tolerance of the calmodulin-peptide binding surface. This may lead to the development of non- or slowly-hydrolysable calmodulin inhibitors that function at the intracellular level. The binding site is the same as that for peptides possessing L-amino acids.

Details

ISSN :
00280836
Volume :
368
Issue :
6472
Database :
Gale General OneFile
Journal :
Nature
Publication Type :
Academic Journal
Accession number :
edsgcl.15469385