A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study(818 views) De Capua A, Del Gatto A, Zaccaro L, Saviano G, Carlucci A, Livigni A, Gedressi C, Tancredi T, Pedone C, Saviano M
Keywords: α-Helix, Akap121, Mitochondrial Targeting (mt) Domain, Synthetic Peptides, Alcohols, Conformations, Data Reduction, Enzyme Kinetics, Mixtures, Molecular Structure, Polypeptides, Motifs, Peptide Reproduction, Trifluoroethanol (tfe), Biopolymers, Cyclic Amp Dependent Protein Kinase, Tubulin, Water, Alpha Helix, Amino Acid Sequence, Amino Terminal Sequence, Circular Dichroism, Conference Paper, Hydrophobicity, Nuclear Magnetic Resonance, Protein Conformation, Protein Domain, Protein Motif, Protein Protein Interaction, Protein Targeting, Structure Analysis, Adaptor Proteins, Signal Transducing, Amino Acid Motifs, Animals, Humans, Models, Molecular Sequence Data, Biomolecular, A Kinase Anchor Proteins, Chemistry, Metabolism, Chemical Synthesis,
Affiliations: *** IBB - CNR ***
Dipartimento di Scienze Ambientali, Seconda Università di Napoli, Caserta, 81100, Italy
Ist. di Biostrutture e Bioimmagini, Dipartimento di Chimica Biologica, Univ. Studi di Napoli Federico II, Napoli, 80134, Italy
Dipto. Sci. e Tecnol. Ambiente e T., Universita degli Studi del Molise, Isernia, 86170, Italy
Dipto. Biol. e Patol. Molec. e Cell., Univ. Studi di Napoli Federico II, Napoli, 80131, Italy
Istituto di Chimica Biomolecolare, CNR, Comprensorio A. Olivetti, via Campki Flegrei 34, Pozzuoli, Napoli, 80078, Italy
References: Not available.
A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study
The conformational features of a peptide derived by the 10-30 sequence of the mitochondrial domain of AKAP121 [Ac-(1)XKKPLALPGMLALLGWWWFFSRKKX(25)-NH2 (X = beta-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 a-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 a-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. (C) 2004 Wiley Periodicals, Inc.
A synthetic peptide reproducing the mitochondrial targeting motif of AKAP121: A conformational study