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首页> 外文期刊>Biochemistry >Effect of Cholesterol on the Membrane Interaction of Modelin-5 Isoforms
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Effect of Cholesterol on the Membrane Interaction of Modelin-5 Isoforms

机译：胆固醇对Modelin-5同工型膜相互作用的影响

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摘要

Modelin-5 isoforms were used to gain an insight into the effects of amidation on antimicrobial selectivity. When tested against Escherichia coli, amidation increased toxicity 10-fold (MIC = 31.25 μM) while showing limited increased hemolytic activity (2% lysis). Our results show that both the amidated and non-amidated peptides had a disordered structure in aqueous solution (<18% helical) and folded to form helices at the membrane interface (for example, >43% in the presence of DMPC). The stabilization of the helical structure by amidation has previously been shown to play a key role in increasing antibacterial efficacy. The presence of cholesterol in the membrane increases the packing density (C_s~(-1) values 25-33 mN m~(-1)) and so prevents the peptide from forming stable association with the membrane, which is evidenced by the higher binding coefficient (K_d) in the presence of cholesterol: 57.70 μM for Modelin-5-COOH and 35.64 μM for Modelin-5-CONH_2 compared to the presence of E. coli lipid extract (10 μM), which would prevent local concentration of the peptide at the bilayer interface as seen by reduction in monolayer interaction. This in turn would be predicted to inhibit activity.
机译：使用Modelin-5同工型来了解酰胺化对抗菌素选择性的影响。当针对大肠杆菌进行测试时，酰胺化将毒性提高了10倍（MIC = 31.25μM），而溶血活性却有限地提高了（裂解率为2％）。我们的结果表明，酰胺化和非酰胺化的肽在水溶液中均具有无序结构（螺旋度小于18％），并在膜界面处折叠形成螺旋（例如在DMPC存在下大于43％）。以前已经显示通过酰胺化来稳定螺旋结构在增加抗菌效力中起关键作用。膜中胆固醇的存在增加了堆积密度（C_s〜（-1）值为25-33 mN m〜（-1）），因此阻止了肽与膜形成稳定的缔合，这可以通过更高的结合力来证明。胆固醇存在下的最大系数（K_d）：与存在大肠杆菌脂质提取物（10μM）相比，Modelin-5-COOH为57.70μM，Modelin-5-CONH_2为35.64μM，这会阻止肽的局部浓缩如通过单层相互作用的减少所见。进而可以预测这会抑制活性。

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