A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study

✍ Scribed by Antonia De Capua; Annarita Del Gatto; Laura Zaccaro; Gabriella Saviano; Annalisa Carlucci; Alessandra Livigni; Chiara Gedressi; Teodorico Tancredi; Carlo Pedone; Michele Saviano

• Publisher: Wiley (John Wiley & Sons)
• Year: 2004
• Tongue: English
• Weight: 199 KB
• Volume: 76
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20146

✦ Synopsis

Abstract

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