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A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study
Author(s) -
De Capua Antonia,
Del Gatto Annarita,
Zaccaro Laura,
Saviano Gabriella,
Carlucci Annalisa,
Livigni Alessandra,
Gedressi Chiara,
Tancredi Teodorico,
Pedone Carlo,
Saviano Michele
Publication year - 2004
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20146
Subject(s) - chemistry , peptide , nuclear magnetic resonance spectroscopy , structural motif , biophysics , protein structure , crystallography , peptide sequence , stereochemistry , biochemistry , biology , gene
The conformational features of a peptide derived by the 10–30 sequence of the mitochondrial domain of AKAP121 [Ac‐ 1 XKKPLALPGMLALLGWWWFFSRKKX 25 ‐NH 2 (X = β‐Ala)] in water and in a water/triflouroethanol (TFE) mixture at 298 K have been determined by NMR and CD spectroscopy. Backbone clustering analysis of NMR‐derived structures led to the identification of a single representative structure in water/TFE. The structure of the peptide consists mainly of an α‐helix, whose core is the region 7–23, with a less ordered N‐terminal part. These data are confirmed by CD analysis. It is noteworthy that the high hydrophobic Trp 16 –Phe 20 segment, that might also mediate interaction with tubulin, is organized in an α‐helical wheel. Our conformational data can be the starting point for the development of highly selective peptides that interfere with the biological function of the Protein Kinase A scaffold protein AKAP121. © 2004 Wiley Periodicals, Inc. Bioploymers (Pept Sci), 2004