作者:Bo Wu、Weiping Zheng
DOI:10.3390/molecules25194506
日期:——
Four bis-lactam [i, i+4]-stapled peptides with d- or l-α-methyl-thialysines were constructed on a model peptide sequence derived from p110α[E545K] and subjected to circular dichroism (CD) and proteolytic stability assessment, alongside the corresponding bis-lactam [i, i+4]-stapled peptide with l-thialysine. The % α-helicity values of these four stapled peptides were found to be largely comparable to
在源自 p110α[E545K] 的模型肽序列上构建了四个具有 d-或 l-α-甲基-硫赖氨酸的双内酰胺 [i, i+4] 钉合肽,并进行圆二色性 (CD) 和蛋白水解稳定性评估, 与相应的双内酰胺 [i, i+4] 钉合肽与 l-硫赖氨酸。发现这四种钉合肽的 % α-螺旋度值在很大程度上彼此相当,但大于具有 l-硫赖氨酸的钉合肽的α-螺旋度值。还发现建立在源自核糖核酸酶 A (RNase A) 的模型肽序列上的 l-α-甲基-硫赖氨酸缝合肽比其 l-硫赖氨酸缝合对应物表现出更大的 α-螺旋%。而且,