吸附
纳米颗粒
形态学(生物学)
胶体金
溶菌酶
蛋白质吸附
结合
纳米棒
材料科学
蛋白质二级结构
化学工程
化学
单层
共价键
结晶学
分子
纳米技术
生物物理学
有机化学
生物化学
工程类
遗传学
数学分析
数学
生物
作者
Jennifer E. Gagner,Marimar D. Lopez,Jonathan S. Dordick,Richard W. Siegel
出处
期刊:Biomaterials
[Elsevier]
日期:2011-10-01
卷期号:32 (29): 7241-7252
被引量:258
标识
DOI:10.1016/j.biomaterials.2011.05.091
摘要
Many biomedical applications of gold nanoparticles (NPs) rely on proteins that are covalently attached or adsorbed on the NP surface. The biological functionality of the protein-NP conjugate depends on the protein’s ability to interact with target molecules, which is affected by NP characteristics such as size, curvature, aspect ratio, morphology, crystal structure, and surface chemistry. In the present study, the effect of gold nanoparticle morphology on the structure and function of adsorbed enzymes, lysozyme (Lyz) and α-chymotrypsin (ChT), has been investigated. Gold nanospheres (AuNS) were synthesized with diameters 10.6 ± 1 nm, and gold nanorods (AuNR) were synthesized with dimensions of (10.3 ± 2) × (36.4 ± 9) nm. Under saturating conditions, proteins adsorb with a higher surface density on AuNR when compared to AuNS. In the case of Lyz, adsorption on AuNS and AuNR resulted in a 10% and 15% loss of secondary structure, respectively, leading to conjugate aggregation and greatly reduced enzymatic activity. ChT retained most of its secondary structure and activity on AuNS and AuNR at low surface coverages; however, as protein loading approached monolayer conditions on AuNR, a 40% loss in secondary structure and 86% loss of activity was observed. Subsequent adsorption of ChT in multilayers on the AuNR surface allowed the conjugates to recover activity and remain stable. It is clear that AuNP morphology does affect adsorbed protein structure; a better understanding of these differences will be essential to engineer fully functional nanobioconjugates.
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