Sulfate ion-triggered self-assembly transitions of amphiphilic short peptides by force balance adjustment

Sulfate ion-triggered self-assembly transitions of amphiphilic short peptides by force balance adjustment
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通过力平衡调节硫酸根离子触发两亲性短肽的自组装转变

DOI:
10.1016/j.colsurfa.2022.128252
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发表时间:
2022-01
期刊:
Colloids and Surfaces A: Physicochemical and Engineering Aspects
影响因子:
--
通讯作者:
Meiwen Cao
Meiwen Cao
中科院分区:
其他
文献类型:
--
作者:
Qun Zhang;Yang Liu;Teng Xie;Yangnan Shang-guan;Maozhang Tian;Qinghua Zhang;Meiwen Cao

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二价硫酸根离子(SO42-)通过调节自组装过程中的力平衡,有效地调控了A6K、A9K和I3K三种结构特征相似但序列不同的两亲性多肽的自组装行为。SO42-与多肽自组装的相互作用使自组装结构的形态发生了明显的变化,这取决于多肽分子的疏水性和自组装结构的稳定性。A6K和A9K产生了新的结构,而I3K没有明显的结构变化。然而,这三种情况的一个共同特征是,盐的添加大大增强了侧向联想倾向。其潜在的机制应该是盐离子有效地调节了不同的自组装驱动力之间的平衡,即静电相互作用、疏水相互作用和氢键,从而触发自组装路线的改变以产生新的结构。这项研究提供了对特定离子效应的新见解,并为调节多肽自组装以精确控制自组装结构铺平了新的途径。
The divalent sulfate ion (SO42-) was found to effectively modulate the self-assembly behaviors of three amphiphilic peptides with similar structural feature but varied sequence, that is, A6K, A9K and I3K, by modulating the force balance during the self-assembly process. Intervening of SO42-with peptide self-assembly resulted in distinct morphology changes of the self-assembled structures depending on the peptide molecular hydrophobicity and the stability of the self-assembled structures. New structures were produced in the cases of A6K and A9K, while no obvious structural change was found for I3K. However, one common feature for the three cases was that the lateral association propensity was greatly enhanced by salt addition. The underlying mechanism should be that the salt ions modulate effectively the balance between different driving forces for self-assembly, that is, electrostatic interaction, hydrophobic interaction and hydrogen bonding, which trigger change of the self-assembly route to produce new structures. The study provides new insights into the specific ion effects and paves new ways for modulating the peptide self-assembly to control precisely the self-assembled structures.
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