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

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

Research output: Contribution to journalArticlepeer-review

Abstract

The conformational features of a peptide derived by the 10-30 sequence of the mitochondrial domain of AKAP121 [Ac-1XKKPLALPGMLALLGWWWFFSRKKX25-NH2 (X=beta-Ala)] in water and in a water/trifluoroethanol (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 alpha-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 Trp16-Phe20 segment, that might also mediate interaction with tubulin, is organized in an alpha-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.
Original languageEnglish
Pages (from-to)459-66
Number of pages8
JournalBiopolymers
Volume76
Issue number6
DOIs
Publication statusPublished - 2004

Keywords

  • A Kinase Anchor Proteins
  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Circular Dichroism
  • Humans
  • Mitochondria
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides
  • Protein Conformation

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