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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Membrane destabilizing activity of influenza virus hemagglutinin-based synthetic peptide: implications of critical glycine residue in fusion peptide.
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Membrane destabilizing activity of influenza virus hemagglutinin-based synthetic peptide: implications of critical glycine residue in fusion peptide.

机译：流感病毒血凝素基合成肽的膜去稳定活性：融合肽中关键甘氨酸残基的影响。

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摘要

Peptide III is a 20-residue synthetic model peptide based on the fusion peptide of influenza virus A/PR/8/34 strain and takes a secondary structure similar to the original peptide. While conserving the amphiphilic helical nature, 20 peptides to modify the bulkiness of side chains of peptide III were synthesized, and acid-induced membrane destabilization was assessed by aqueous content leakage from large unilamellar vesicles. Substitutions on the hydrophobic side decreased activity but showed less effect on the hydrophilic side, which confirmed the importance of the hydrophobic side for interaction with the membrane. Interestingly, substitution at the 13th Gly residue enhanced the amphiphilic helical nature but severely reduced activity. Correlation between alpha-helical content at acidic pH and the activity was not recognized, suggesting rather that the importance of this site was due to helix termination by glycine which allows N-terminal and C-terminal halves to behave as different secondary structural units.
机译：肽III是20个残基的合成模型肽，基于流感病毒A / PR / 8/34菌株的融合肽，并具有与原始肽相似的二级结构。在保持两亲螺旋性质的同时，合成了20种修饰肽III侧链的大体积的肽，并通过从大单层囊泡中的含水量泄漏来评估酸诱导的膜失稳。疏水侧上的取代降低了活性，但是对亲水侧上显示的作用较小，这证实了疏水侧对于与膜相互作用的重要性。有趣的是，在第13 Gly残基处的取代增强了两亲性螺旋性质，但活性大大降低。酸性pH值下的α-螺旋含量与活性之间没有相关性，这表明该位点的重要性是由于甘氨酸终止螺旋，使N-末端和C-末端半部分表现为不同的二级结构单元。

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