Interaction of β-Amyloid Interactions with Peptide Functionalized Gold Nanoparticles

被引:11
|
作者
Hemmaragala, Nanjundaswamy M. [1 ]
Arvidsson, Per I. [2 ,3 ,4 ]
Maguire, Glenn E. M. [1 ]
Kruger, Hendrik G. [1 ]
Govender, Thavendran [2 ]
机构
[1] Univ KwaZulu Natal, Sch Chem, ZA-4001 Durban, South Africa
[2] Univ KwaZulu Natal, Sch Pharm & Pharmacol, ZA-4001 Durban, South Africa
[3] Uppsala Univ, Dept Med Chem, Uppsala Biomed Ctr, SE-75123 Uppsala, Sweden
[4] AstraZeneca R&D Sodertalje, Innovat Med, CNSP iMed, S-15185 Sodertalje, Sweden
关键词
Gold Nanoparticles (GNPs); Peptides; Resonance Spectroscopy; beta-Amyloid (A beta); ALZHEIMERS-DISEASE; FIBRIL FORMATION; IN-VITRO; NANOTECHNOLOGY; AGENTS; IMMUNOSENSOR; INHIBITORS; TOXICITY; DELIVERY; DESIGN;
D O I
10.1166/jnn.2012.5791
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:2179 / 2184
页数:6
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