Effect of hydrophobic amino acids on the conformational change of decapeptides in micellar environments |
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Authors: | Junko Kuwahara Hideo Akisada Tamaki Kato Norikazu Nishino |
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Institution: | (1) Department of Environmental Chemistry, Faculty of Engineering, Kyushu Kyoritsu University, Kitakyushu 807-8585, Japan;(2) Graduate School of Life Science and Systems Engineering, Kyushu Institute of Technology, Kitakyushu 808-0196, Japan;(3) Faculty of Engineering, Kyushu Institute of Technology, Kitakyushu 808-8550, Japan |
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Abstract: | 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 -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 -helices in micellar environments. The conformational transition from -helix to -sheet structure required moderate hydrophobicity and linear side chains. This conformational transition depended on the surfactant concentration. |
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Keywords: | Peptide Micelle -Helix" target="_blank">gif" alt="agr" align="BASELINE" BORDER="0">-Helix -Sheet" target="_blank">gif" alt="beta" align="MIDDLE" BORDER="0">-Sheet Norleucine |
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