Lin Wayne, Insley Thomas, Tuttle Marcus D, Zhu Lingyang, Berthold Deborah A, Král Petr, Rienstra Chad M, Murphy Catherine J
Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Matthews Avenue, Urbana, Illinois, 61801, USA.
Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, Illinois, 60607, USA.
J Phys Chem C Nanomater Interfaces. 2015 Sep 10;119(36):21035-21043. doi: 10.1021/acs.jpcc.5b07701. Epub 2015 Aug 18.
Gold nanoparticles (Au NPs) have attracted much attention due to their potential applications in nano-medicine. While numerous studies have quantified biomolecular adsorption to Au NPs in terms of equilibrium binding constants, far less is known about biomolecular orientation on nanoparticle surfaces. In this study, the binding of the protein α-synuclein to citrate and (16-mercaptohexadecyl) trimethylammonium bromide (MTAB) coated 12 nm Au NPs is examined by heteronuclear single quantum coherence NMR spectroscopy to provide site-specific measurements of protein-nanoparticle binding. Molecular dynamics simulations support the orientation assignments, which show N-terminus binding to the Au NP for citrate-capped NPs, and C-terminus binding for the MTAB-capped NPs.
金纳米颗粒（Au NPs）因其在纳米医学中的潜在应用而备受关注。虽然许多研究已根据平衡结合常数对生物分子在金纳米颗粒上的吸附进行了量化，但对于纳米颗粒表面生物分子的取向却知之甚少。在本研究中，通过异核单量子相干核磁共振光谱研究了蛋白质α-突触核蛋白与柠檬酸盐和（16-巯基十六烷基）三甲基溴化铵（MTAB）包覆的12纳米金纳米颗粒的结合，以提供蛋白质-纳米颗粒结合的位点特异性测量。分子动力学模拟支持了取向分配，结果表明，对于柠檬酸盐包覆的纳米颗粒，N端与金纳米颗粒结合；对于MTAB包覆的纳米颗粒，C端与金纳米颗粒结合。
