Effect of gold nanoparticle morphology on adsorbed protein structure and function
Effect of gold nanoparticle morphology on adsorbed protein structure and function
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DOI：
10.1016/j.biomaterials.2011.05.091
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发表时间：
2011-10-01
期刊：
影响因子：
14
通讯作者：
Siegel, Richard W.
中科院分区：
文献类型：
--
作者：
Gagner, Jennifer E.;Lopez, Marimar D.;Siegel, Richard W.
金纳米颗粒（NPs）的许多生物医学应用依赖于共价附着或吸附在纳米颗粒表面的蛋白质。蛋白质-NP偶联物的生物学功能取决于蛋白质与靶分子相互作用的能力，而这种能力受NP特征（如大小、曲率、纵横比、形态、晶体结构和表面化学）的影响。在本研究中，研究了金纳米颗粒形态对吸附酶溶菌酶（Lyz）和α -凝乳胰蛋白酶（ChT）结构和功能的影响。制备了直径为10.6 +/- 1 nm的金纳米球（AuNS）和尺寸为（10.3 +/- 2）x (36.4 +/- 9) nm的金纳米棒（AuNR）。在饱和条件下，与金纳米棒相比，蛋白质在AuNR上的吸附表面密度更高。以Lyz为例，吸附在AuNS和AuNR上分别导致10%和15%的二级结构损失，导致共轭聚集，酶活性大大降低。在低地表覆盖度条件下，ChT在aun和unr上保留了大部分二级结构和活性；然而，当蛋白质在AuNR上加载接近单层条件时，二级结构损失40%，活性损失86%。随后在AuNR表面多层吸附ChT，使共轭物恢复活性并保持稳定。很明显，AuNP的形态确实影响吸附的蛋白质结构；更好地了解这些差异对于设计功能齐全的纳米生物偶联物至关重要。(C) 2011 Elsevier Ltd.版权所有。
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 alpha-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) x (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. (C) 2011 Elsevier Ltd. All rights reserved.