Agricultural Nanocenter, School of Life Science, Inner Mongolia Agricultural University , 306 Zhaowuda Road, Hohhot 010018, China.
ACS Appl Mater Interfaces. 2016 Feb 3;8(4):2478-85. doi: 10.1021/acsami.5b08386. Epub 2016 Jan 20.
The robust physisorption between nanoparticles (NPs) and proteins has attracted increasing attention due to the significance for both conjugation techniques and protein's corona formation at the bionano interface. In the present study, we first explored the possible binding sites of the bovine serum albumin (BSA) on amphiphilic polymer coated gold nanoparticles (AP-AuNPs). By using mass spectrometry, a 105-amino-acid peptide (12.2 kDa) is discovered as the possible "epitope" responsible for the robust physisorption between BSA and AP-AuNPs. Second, with the help of nanometal surface energy transfer (NSET) theory, we further found that the epitope peptide could insert at least 2.9 nm into the organic molecular layers of AP-AuNPs when the robust conjugates formed, which indicates how such a long epitope peptide can be accommodated by AP-AuNPs and resist protease's digestion. These findings might shed light on a new strategy for studying interactions between proteins and NPs, and further guide the rational design of NPs for safe and effective biomedical applications.
由于纳米粒子（NPs）与蛋白质之间的强物理吸附在连接技术和生物纳米界面上蛋白质的冠形成方面具有重要意义，因此引起了越来越多的关注。在本研究中，我们首先探索了牛血清白蛋白（BSA）在两亲聚合物包覆的金纳米粒子（AP-AuNPs）上的可能结合位点。通过使用质谱法，发现了一个由 105 个氨基酸组成的肽（12.2 kDa）可能是 BSA 与 AP-AuNPs 之间强物理吸附的“抗原决定簇”。其次，借助纳米金属表面能量转移（NSET）理论，我们进一步发现，当形成强缀合物时，抗原决定簇肽至少可以插入 AP-AuNPs 的有机分子层 2.9nm，这表明如此长的抗原决定簇肽如何可以被 AP-AuNPs 容纳并抵抗蛋白酶的消化。这些发现可能为研究蛋白质与 NPs 之间的相互作用提供新的策略，并进一步指导 NPs 的合理设计，以实现安全有效的生物医学应用。
