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β-淀粉样蛋白与肽功能化金纳米颗粒的相互作用。

Interaction of beta-amyloid interactions with peptide functionalized gold nanoparticles.

作者信息

Hemmaragala Nanjundaswamy M, Arvidsson Per I, Maguire Glenn E M, Kruger Hendrik G, Govender Thavendran

机构信息

School of Chemistry, University of KwaZulu Natal, Durban 4001, South Africa.

出版信息

J Nanosci Nanotechnol. 2012 Mar;12(3):2179-84. doi: 10.1166/jnn.2012.5791.

Abstract

The physicochemical properties of gold nanoparticles (GNPs) functionalized with peptides and N-methylated peptides were studied with respect to their interaction with beta-amyloid (1-42). Peptides with sequences of CGGIGLMVG and CGGGGGIGLMVG linked with GNPs of an average diameter of 13 nm were employed for this study. The peptide-GNPs were found to be soluble and dispersed at pH 7.4 in a sodium phosphate aqueous buffer solution. The resonance spectra of each peptide coated GNP was measured in the absence and presence of beta-amyloid (1-42). The difference in the intensity of the lambda(max) of the resonance absorption bands was attributed to the interaction of the functionalized GNPs with the protein. Particles bearing the CGGGGGIGLMVG sequence exhibited the largest change in lambda(max) intensity; the prevention of fibril formation and inhibition of cytotoxicity was also examined.

摘要

研究了用肽和N-甲基化肽功能化的金纳米颗粒(GNP)与β-淀粉样蛋白(1-42)相互作用的物理化学性质。本研究采用与平均直径为13nm的GNP相连的序列为CGGIGLMVG和CGGGGGIGLMVG的肽。发现肽-GNP在pH 7.4的磷酸钠水溶液缓冲液中可溶且分散。在不存在和存在β-淀粉样蛋白(1-42)的情况下测量了每个肽包被的GNP的共振光谱。共振吸收带λ(max)强度的差异归因于功能化GNP与蛋白质的相互作用。带有CGGGGGIGLMVG序列的颗粒在λ(max)强度上表现出最大变化;还研究了对原纤维形成的预防和细胞毒性的抑制。

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