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首页> 外文期刊>Biochemistry >Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles
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Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles

机译：转运蛋白10的一级结构的微小变化改变了其与磷脂囊泡相互作用的热力学和动力学。

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摘要

The kinetics and thermodynamics of binding of transportan 10 (tp10) and four of its variants to phospholipid vesicles, and the kinetics of peptide-induced dye efflux, were compared. Tp10 is a 21-residue, amphipathic, cationic, cell-penetrating peptide similar to helical antimicrobial peptides. The tp10 variants examined include amidated and free peptides, and replacements of tyrosine by tryptophan. Carboxyterminal amidation or substitution of tryptophan for tyrosine enhance binding and activity. The Gibbs energies of peptide binding to membranes determined experimentally and calculated from the interfacial hydrophobicity scale are in good agreement. The Gibbs energy for insertion into the bilayer core was calculated using hydrophobicity scales of residue transfer from water to octanol and to the membrane/water interface. Peptide-induced efflux becomes faster as the Gibbs energies for binding and insertion of the tp10 variants decrease. If anionic lipids are included, binding and efflux rate increase, as expected because all tp10 variants are cationic and an electrostatic component is added. Whether the most important effect of peptide amidation is the change in charge or an enhancement of helical structure, however, still needs to be established. Nevertheless, it is clear that the changes in efflux rate reflect the differences in the thermodynamics of binding and insertion of the free and amidated peptide groups.
机译：比较了运链蛋白10（tp10）及其四个变体与磷脂囊泡结合的动力学和热力学，以及肽诱导的染料外排的动力学。 Tp10是一种21残基，两亲性，阳离子性，可穿透细胞的肽，类似于螺旋抗菌肽。检查的tp10变体包括酰胺化和游离肽，以及酪氨酸被色氨酸替代。羧基末端酰胺化或色氨酸取代酪氨酸可增强结合和活性。实验确定并根据界面疏水性尺度计算的肽与膜结合的吉布斯能很好地吻合。使用残基从水转移到辛醇以及转移到膜/水界面的疏水性比例，计算了插入双层核的吉布斯能量。随着tp10变体的结合和插入的吉布斯能量降低，肽诱导的外排变得更快。如果包括阴离子脂质，则如预期的那样，结合和流出速率会增加，因为所有的tp10变体都是阳离子的，并且添加了静电成分。然而，仍然需要确定肽酰胺化的最重要作用是电荷的改变还是螺旋结构的增强。然而，很明显，流出速率的变化反映了游离和酰胺化肽基团的结合和插入的热力学差异。

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