Redox Activity of Copper(II) Complexes with NSFRY Pentapeptide and Its Analogues
| Autor: | Grzegorz Piotrowski, Urszula E. Wawrzyniak, Arkadiusz Bonna, Wojciech Wróblewski, Iwona Ufnalska, Magdalena Z. Wiloch |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Molecular model Protein Conformation lcsh:Medicine Peptide Physical Chemistry Biochemistry 01 natural sciences Pentapeptide repeat Aromatic Amino Acids Protein structure Drug Stability Electrochemistry Metalloprotein Amino Acids lcsh:Science chemistry.chemical_classification Multidisciplinary Organic Compounds Chemical Reactions Chemical Synthesis Chemistry Physical Sciences Oxidation-Reduction Atrial Natriuretic Factor Research Article Protein Binding Biosynthetic Techniques Stereochemistry Phenylalanine chemistry.chemical_element Research and Analysis Methods 010402 general chemistry Redox Structure-Activity Relationship Hydroxyl Amino Acids Cations Humans Structure–activity relationship Peptide Synthesis Ions Binding Sites 010405 organic chemistry Electrode Potentials lcsh:R Organic Chemistry Chemical Compounds Biology and Life Sciences Proteins Copper Peptide Fragments 0104 chemical sciences chemistry Tyrosine lcsh:Q Oxidation-Reduction Reactions |
| Zdroj: | PLoS ONE PLoS ONE, Vol 11, Iss 8, p e0160256 (2016) |
| ISSN: | 1932-6203 |
| Popis: | The influence of cation-π interactions on the electrochemical properties of copper(II) complexes with synthesized pentapeptide C-terminal fragment of Atrial Natriuretic Factor (ANF) hormone was studied in this work. Molecular modeling performed for Cu(II)-NSFRY-NH2 complex indicated that the cation-π interactions between Tyr and Cu(II), and also between Phe-Arg led to specific conformation defined as peptide box, in which the metal cation is isolated from the solvent by peptide ligand. Voltammetry experiments enabled to compare the redox properties and stability of copper(II) complexes with NSFRY-NH2 and its analogues (namely: NSFRA-NH2, NSFRF-NH2, NSAAY-NH2, NSAAA-NH2, AAAAA-NH2) as well as to evaluate the contribution of individual amino acid residues to these properties. The obtained results led to the conclusion, that cation-π interactions play a crucial role in the effective stabilization of copper(II) complexes with the fragments of ANF peptide hormone and therefore could control the redox processes in other metalloproteins. |
| Databáze: | OpenAIRE |
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