Specific Ion Interaction Dominates over Hydrophobic Matching Effects in Peptide–Lipid Bilayer Interactions: The Case of Short Peptide
Specific Ion Interaction Dominates over Hydrophobic Matching Effects in Peptide–Lipid Bilayer Interactions: The Case of Short Peptide
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DOI：
10.1021/jp411413u
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发表时间：
2013-12
影响因子：
3.7
通讯作者：
Feng Wei;Hongchun Li;Shuji Ye
中科院分区：
文献类型：
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作者：
Feng Wei;Hongchun Li;Shuji Ye
将短肽插入细胞膜在能量上是不利的，并且挑战了普遍接受的疏水匹配原则。然而，已有证据表明，在盐溶液中，许多短肽可以穿透到细胞内发挥生物学功能。在前人研究的基础上(J.Phys.化学。C 2013,117,11095−11103)，在此，我们进一步系统地研究了马斯多兰与不同脂链长度的中性脂双层之间的相互作用，并利用和频产生振动光谱考察了不同水盐环境下的疏水匹配原理。研究发现，在纯水环境中，疏水匹配是MP与脂质双层缔合的主要驱动力。然而，在共渗离子环境中，离子的水合作用可以克服疏水失配效应，导致MP插入到具有更长疏水长度的脂双层中。当它……
Insertion of short peptides into the cell membrane is energetically unfavorable and challenges the commonly accepted hydrophobic matching principle. Yet there has been evidence that many short peptides can penetrate into the cells to perform the biological functions in salt solution. On the basis of the previous study (J. Phys. Chem. C 2013, 117, 11095−11103), here we further performed a systematic study on the interaction of mastoparan with various neutral lipid bilayers with different lipid chain lengths in situ to examine the hydrophobic matching principle in different aqueous salt environments using sum frequency generation vibrational spectroscopy. It is found that the hydrophobic matching is the dominant driving force for the association of MP with a lipid bilayer in a pure water environment. However, in a kosmotropic ion environment, the hydration of ions can overcome the hydrophobic mismatching effects, leading to the insertion of MP into lipid bilayers with much longer hydrophobic lengths. When t...