Deletion of the Carboxyl-Terminal Residue Disrupts the Amino-Terminal Folding, Self-Association and Thermal Stability of an Amphipathic Antimicrobial Peptide

doi:10.1002/psc.2635

淡江大學機構典藏 > 理學院 > 化學學系暨研究所 > 期刊論文 > Item 987654321/96156

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题名:	Deletion of the Carboxyl-Terminal Residue Disrupts the Amino-Terminal Folding, Self-Association and Thermal Stability of an Amphipathic Antimicrobial Peptide
作者:	李長欣
贡献者:	淡江大學化學學系
关键词:	antimicrobial peptide;diffusion;enthalpic interaction;self-association;thermal stability
日期:	2014-04-24
上传时间:	2014-03-05 10:10:40 (UTC+8)
摘要:	Understanding the complex relationship between amino acid sequence and protein behaviors, such as folding and self-association, is a major goal of protein research. In the present work, we examined the effects of deleting a C-terminal residue on the intrinsic properties of an amphapathic α-helix of mastoparan-B (MP-B), an antimicrobial peptide with the sequence LKLKSIVSWAKKVL-NH2. We used circular dichroism and nuclear magnetic resonance to demonstrate that the peptide MP-B[1-13] displayed significant unwinding at the N-terminal helix compared with the parent peptide of MP-B, as the temperature increased when the residue at position 14 was deleted. Pulsed-field gradient nuclear magnetic resonance data revealed that MP-B forms a larger diffusion unit than MP-B[1-13] at all experimental temperatures and continuously dissociates as the temperature increases. In contrast, the size of the diffusion unit of MP-B[1-13] is almost independent of temperature. These findings suggest that deleting the flexible, hydrophobic amino acid from the C-terminus of MP-B is sufficient to change the intrinsic helical thermal stability and self-association. This effect is most likely because of the modulation of enthalpic interactions and conformational freedom that are specified by this residue. Our results implicate terminal residues in the biological function of an antimicrobial peptide. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
關聯:	Journal of Peptide Science 20(6),　p.438-445
DOI:	10.1002/psc.2635
显示于类别:	[化學學系暨研究所] 期刊論文

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