Analysis of the Dynamics of Assembly and Structural Impact for a Histidine Tagged FGF1−1.5 nm Au Nanoparticle Bioconjugate

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• 作者：Joshua M. Kogot ; Alex M. Parker ; Jihun Lee ; Michael Blaber ; Geoffrey F. Strouse ; Timothy M. Logan
• 刊名：Bioconjugate Chemistry
• 出版年：2009
• 出版时间：November 18, 2009
• 年：2009
• 卷：20
• 期：11
• 页码：2106-2113
• 全文大小：297K
• 年卷期：v.20,no.11(November 18, 2009)
• ISSN：1520-4812

文摘

Whether assembling proteins onto nanoscale, mesoscopic, or macroscropic material surfaces, maintaining a protein’s structure and function when conjugated to a surface is complicated by the high propensity for electrostatic or hydrophobic surface interactions and the possibility of direct metal coordination of protein functional groups. In this study, the assembly of a 1.5 nm CAAKA passivated gold nanoparticle (AuNP) onto FGF1 (human acidic fibroblast growth factor) using an amino terminal His₆ tag is analyzed. The impact of structure and time-dependent changes in the structural elements in FGF1and FGF1-heparin in the presence of the AuNP is probed by a molecular beacon fluorescence assay, circular dichroism, and NMR spectroscopy. Analysis of the results indicates that a time-dependent evolution of the protein structure without loss of FGF1 heparin binding occurs following the formation of the initial FGF1-AuNP complex. The time-dependent changes are believed to reflect protein sampling of the AuNP surface to minimize the free energy of the AuNP-FGF1 complex without impacting FGF1 function.