生物结合
化学
牛血清白蛋白
试剂
胶体金
人血清白蛋白
血清白蛋白
纳米颗粒
蛋白质吸附
表面改性
组合化学
药物输送
吸附
色谱法
纳米技术
生物化学
有机化学
材料科学
物理化学
作者
Tosin Ogunlusi,Jeremy D. Driskell
出处
期刊:Langmuir
[American Chemical Society]
日期:2023-03-01
卷期号:39 (10): 3720-3728
被引量:1
标识
DOI:10.1021/acs.langmuir.2c03429
摘要
Proteins adsorbed to gold nanoparticles (AuNPs) form bioconjugates and are critical to many emerging technologies for drug delivery, diagnostics, therapies, and other biomedical applications. A thorough understanding of the interaction between the immobilized protein and AuNP is essential for the bioconjugate to perform as designed. Here, we explore a correlation between the number of solvent-accessible thiol groups on a protein and the protein desorption rate from the AuNP surface in the presence of a competing protein. The chemical modification of human serum albumin (HSA) was carried out to install additional free thiols using Traut's reagent and create a library of HSA analogues by tailoring the molar excess of the Traut's reagent. We pre-adsorbed HSA variants onto the AuNP surface, and the resulting bioconjugates were then exposed to IgG antibody, and protein exchange was monitored as a function of time. We found that the rate of HSA displacement from the AuNP correlated with the experimentally measured number of accessible free thiol groups. Additionally, bioconjugates were synthesized using thiolated analogues of bovine serum albumin (BSA) and suspended in serum as a model for a complex sample matrix. Similarly, desorption rates with serum proteins were modulated with solvent-accessible thiols on the immobilized protein. These results further highlight the key role of Au-S bonds in the formation of protein-AuNP conjugates and provide a pathway to systematically control the number of free thiols on a protein, enabling the controlled release of protein from the surface of AuNP.
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