Effect of hydrophobic amino acids on the conformational change of decapeptides in micellar environments
| Autor: | Tamaki Kato, Hideo Akisada, Norikazu Nishino, Junko Kuwahara |
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| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Conformational change Polymers and Plastics Stereochemistry Norleucine Phenylalanine Peptide Micelle Amino acid chemistry.chemical_compound Colloid and Surface Chemistry chemistry Materials Chemistry Side chain Organic chemistry Physical and Theoretical Chemistry |
| Zdroj: | Colloid and Polymer Science. 283:747-752 |
| ISSN: | 1435-1536 0303-402X |
| DOI: | 10.1007/s00396-004-1217-x |
| Popis: | A series of peptides containing various hydrophobic amino acids [methionine (Met), leucine (Leu), norleucine (Nle), phenylalanine (Phe), 2-aminooctanoic acid (Aoc), and 2-aminodecanoic acid (Ade)] were synthesized and their conformations were studied using circular dichroism (CD) spectroscopy in different solvents such as water, methanol, and aqueous solution of ammonium tetradecanesulfonate. Peptides containing hydrophobic amino acids with linear side chains formed β-sheets in water and methanol. Electrostatic interaction between the charged side chain (lysine) and a micelle consisting of an anionic surfactant, ammonium tetradecanesulfonate, is necessary for the formation of α-helices in micellar environments. The conformational transition from α-helix to β-sheet structure required moderate hydrophobicity and linear side chains. This conformational transition depended on the surfactant concentration. |
| Databáze: | OpenAIRE |
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