蛋白质与聚酰胺-胺型（PAMAM）纳米颗粒的缀合：微观和热力学分析
Protein conjugation with PAMAM nanoparticles: Microscopic and thermodynamic analysis.
作者信息
Chanphai P, Froehlich E, Mandeville J S, Tajmir-Riahi H A
机构信息
Department of Chemistry-Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, TR (Quebec) Canada G9A 5H7, Canada.
Department of Chemistry-Biochemistry and Physics, University of Québec at Trois-Rivières, C. P. 500, TR (Quebec) Canada G9A 5H7, Canada.
出版信息
Colloids Surf B Biointerfaces. 2017 Feb 1;150:168-174. doi: 10.1016/j.colsurfb.2016.11.037. Epub 2016 Nov 27.
PAMAM dendrimers form strong protein conjugates that are used in drug delivery systems. We report the thermodynamic and binding analysis of polyamidoamine (PAMAM-G4) conjugation with human serum albumin (HSA), bovine serum albumin (BSA) and milk beta-lactoglobulin (b-LG) in aqueous solution at physiological pH. Hydrophobicity played a major role in PAMAM-protein interactions with more hydrophobic b-LG forming stronger polymer-protein conjugates. Thermodynamic parameters showed PAMAM-protein bindings occur via hydrophobic and H-bonding contacts for b-LG, while van der waals and H-bonding interactions prevail in HSA and BSA-polymer conjugates. The protein loading efficacy was 45-55%. PAMAM complexation induced major alterations of protein conformation. TEM images show major polymer morphological changes upon protein conjugation.
聚酰胺-胺（PAMAM）树枝状大分子可形成用于药物递送系统的强蛋白质缀合物。我们报道了在生理pH值的水溶液中，聚酰胺-胺（PAMAM-G4）与人血清白蛋白（HSA）、牛血清白蛋白（BSA）和乳β-乳球蛋白（b-LG）缀合的热力学和结合分析。疏水性在PAMAM与蛋白质的相互作用中起主要作用，疏水性更强的b-LG形成更强的聚合物-蛋白质缀合物。热力学参数表明，PAMAM与b-LG的结合通过疏水和氢键接触发生，而在HSA和BSA-聚合物缀合物中，范德华力和氢键相互作用占主导。蛋白质负载效率为45-55%。PAMAM络合引起蛋白质构象的主要改变。透射电子显微镜（TEM）图像显示蛋白质缀合后聚合物形态发生重大变化。
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