期刊
LANGMUIR
卷 29, 期 35, 页码 10990-10996出版社
AMER CHEMICAL SOC
DOI: 10.1021/la402239h
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资金
- NSF CAREER [CHE 1151057]
- NSF [EPS-0903787]
- Agricultural Research Service
- U.S. Department of Agriculture [5864022729]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1151057] Funding Source: National Science Foundation
- EPSCoR
- Office Of The Director [0903787] Funding Source: National Science Foundation
The role of cysteine residues in the. protein binding kinetics and stability. on gold nanoparticles (AuNP) was studied using AuNP: localized surface plasmon resonance (LSPR): in combination with an organothiol (OT) displacement Method. GB3, the third IgG-binding domain of protein G, was used to model protein-AuNP adsorption. While wild.. type GB3 (GB3(0)) contains no cysteine residues, bioengineered GB3 variants containing one (GB3,) and two (GB3(2)) cysteine residues Were also tested: The cysteine content has no significant effect on GB3 binding kinetics with AuNPs, and most protein adsorption occurs within the first few seconds upon protein/AuNP mixing. However, the stability of GB3 on the AuNP surface against OT displacement depends strongly on the cysteine content and the age of the AuNP/GB3 mixture. The GB30 covered AuNPs can be completely destabilized and aggregated by OTs, regardless of the age of the GB3(0)/AuNP mixtures. Long-time incubation of GB3(1) or GB32 with AuNPs can stabilize AuNPs against the OT adsorption inducted aggregation. This study indicates that multiple forces involved in the GB3/AtiNP interaction, and covalent binding between cysteine and AuNP is essential for a stable protein/AuNP complex.
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