Soft Matter Research Center, Department of Chemistry, Zhejiang University, Hangzhou, 310027, PR China.
College of Pharmacy, Binzhou Medical University, Yantai, 264003, PR China.
Mol Inform. 2017 May;36(5-6). doi: 10.1002/minf.201600069. Epub 2016 Dec 22.
Peptides with an exposed arginine-glycine-aspartate (Arg-Gly-Asp, RGD) sequence targeting the integrin α β play an important role in targeted anticancer drug delivery. The interaction of multiple RGD-containing peptides and two α β molecules was studied via MD simulation. Results revealed that not all six RGD-containing peptides interact with α β and interaction strengths differed among the peptides. The specific identification sites included the guanidine group of the ARG residue in the RGD peptide and the carboxyl group of the ASP residue in integrin α β . Therefore, formation of a salt bridge between ARG and the ASP residue was the main mechanism of interaction. H-bonds also played an important role in the observed interaction. The interaction between RGD-containing peptides and α β was influenced by two factors: the relative orientation and distance between these groups. The RGD cluster, which could markedly increase the number of absorbed RGD monomers and enhance the cellular uptake of nano-medicines, was observed in this system.
具有暴露的精氨酸-甘氨酸-天冬氨酸（Arg-Gly-Asp，RGD）序列的肽靶向整合素αβ在靶向抗癌药物输送中起着重要作用。通过 MD 模拟研究了多个含 RGD 的肽与两个αβ分子的相互作用。结果表明，并非所有六个含 RGD 的肽都与αβ相互作用，并且肽之间的相互作用强度不同。特定的识别位点包括 RGD 肽中 ARG 残基的胍基和整合素αβ中 ASP 残基的羧基。因此，ARG 和 ASP 残基之间形成盐桥是相互作用的主要机制。氢键在观察到的相互作用中也起着重要作用。含 RGD 的肽与αβ之间的相互作用受两个因素的影响：这些基团之间的相对取向和距离。在该系统中观察到 RGD 簇，其可以显著增加吸收的 RGD 单体的数量并增强纳米药物的细胞摄取。
