Trifluoroacetic acid as excipient destabilizes melittin causing the selective aggregation of melittin within the centrin-melittin-trifluoroacetic acid complex.
Trifluoroacetic acid as excipient destabilizes melittin causing the selective aggregation of melittin within the centrin-melittin-trifluoroacetic acid complex.
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DOI：
10.1063/1.4921219
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发表时间：
2015-07
期刊：
影响因子：
--
通讯作者：
Santiago J
中科院分区：
文献类型：
--
作者：
Pastrana-Rios B;Del Valle Sosa L;Santiago J
三氟乙酸（TFA）可能是蛋白质-肽复合物高分辨结构测定的瓶颈。基于片段的药物设计通常涉及使用含有TFA（赋形剂）的合成肽。我们的目标是探索这种赋形剂对模型复合物：中心蛋白-蜂毒肽-TFA的影响。我们进行了傅里叶变换红外光谱，二维红外相关光谱和光谱模拟分析的组分和三元复合物的酰胺I '/I'* 带。蜂毒肽（MLT）被观察到具有增加的螺旋后，其与中心蛋白的相互作用，随后由热诱导的聚集MLT在三元复合物中的TFA的存在。
Trifluoroacetic acid (TFA) may be the cause of the bottleneck in high resolution structure determination for protein-peptide complexes. Fragment based drug design often involves the use of synthetic peptides which contain TFA (excipient). Our goal was to explore the effects of this excipient on a model complex: centrin-melittin-TFA. We performed Fourier transform infrared, two-dimensional infrared correlation spectroscopies and spectral simulations to analyze the amide I'/I'* band for the components and the ternary complex. Melittin (MLT) was observed to have increased helicity upon its interaction with centrin, followed by the thermally induced aggregation of MLT within the ternary complex in the TFA presence.