The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism
The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism
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DOI：
10.1002/psc.773
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发表时间：
2006-10-01
影响因子：
2.1
通讯作者：
Kita, Yoshiko
中科院分区：
文献类型：
--
作者：
Arakawa, Tsutomu;Niikura, Takako;Kita, Yoshiko
通过圆二色性（CD）检测了抗阿尔茨海默病肽的高效Ser14Gly类似物Humanin的结构。二级结构在水中比在磷酸盐缓冲盐水（PBS）中更无序。多肽在水中的结构对多肽浓度和温度的依赖性很小。相反，PBS中的肽结构与水中的结构有显著差异，这种差异在更高的肽浓度和温度下更为明显。在PBS中观察到的不同结构似乎是由于肽的自结合，这种自结合通过温度升高而增强，因此通过疏水相互作用。野生型Humanin也表现出类似的行为，即它在水中呈无序结构，但在PBS中发生构象变化。虽然在体内没有遇到用于CD测量的高肽浓度，但结果表明肽倾向于与其他结构以及与自身疏水相互作用。版权所有(c) 2006欧洲多肽协会和约翰威利父子有限公司。
The structure of a highly potent Ser14Gly analog of antiAlzheimer peptide, Humanin, was examined by circular dichroism (CD). The secondary structure is more disordered in water than in phosphate-buffered saline (PBS). The peptide structure in water is little dependent on both peptide concentration and temperature. On the contrary, the peptide structure was significantly different in PBS from the structure in water, which is more apparent at a higher peptide concentration and temperature. The observed different structure in PBS appears to be due to self-association of the peptide, which is enhanced by elevated temperature and, hence, via hydrophobic interactions. The wild-type Humanin also behaved similarly, i.e., it assumed a disordered structure in water but underwent conformational changes in PBS. Although high peptide concentrations for CD measurements are not encountered in vivo, the results suggest the tendency of the peptide to interact hydrophobically with other structures as well as with itself. Copyright (c) 2006 European Peptide Society and John Wiley & Sons, Ltd.