Theoretical analysis of adsorption thermodynamics for hydrophobic peptide residues on SAM surfaces of varying functionality
Theoretical analysis of adsorption thermodynamics for hydrophobic peptide residues on SAM surfaces of varying functionality
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DOI：
10.1002/jbm.10052
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发表时间：
2002-06-15
期刊：
影响因子：
--
通讯作者：
Rini, CJ
中科院分区：
文献类型：
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作者：
Latour, RA;Rini, CJ
在基本水平上，蛋白质在合成表面的吸附必须受到蛋白质表面呈现的多肽残基(初级蛋白质结构)和合成表面呈现的官能团之间的相互作用的强烈影响。在这项研究中，半经验分子模型与实验润湿数据一起被用来从理论上接近蛋白质在这个一级结构水平上的吸附。计算了金[Au-S(CH2)(15)-X；X=CH3，OH，NH3+CoO-]在烷硫醇自组装单分子膜上吸附单个疏水性多肽残基(缬氨酸、亮氨酸、苯丙氨酸)时的热变、熵和吉布斯自由能随残基-表面分离距离的变化。结果表明，每种疏水残基在甲基端疏水表面上的吸附都是能量有利的且以熵为主，在端羟基的中性亲水表面上吸附是不利的且以热能为主，而在带电表面上则是非常微弱的不利吸附和以热能为主的吸附。这些理论结果为理解蛋白质在合成表面吸附的一些基本效应提供了基础。这一水平的理解对于主动设计表面以控制植入和组织工程应用中的蛋白质吸附和随后的细胞反应是必要的。(C)2002年威利期刊公司。
At a fundamental level, protein adsorption to a synthetic surface must be strongly influenced by the interaction between the peptide residues presented v the protein's surface (primary protein structure) and the functional groups presented by the synthetic surface. In this study, semi-empirical molecular modeling was used along with experimental wetting data to theoretically approach protein adsorption at this primary structural level. Changes in enthalpy, entropy, and Gibbs free energy were calculated as a function of residue-surface separation distance for the adsorption of individual hydrophobic peptide residues (valine, leucine, phenylalanine) on alkanethiol self-assembled monolayers on gold [Au-S(CH2)(15)-X; X = CH3, OH, NH3+ COO-]. The results predict that the adsorption of each type of hydrophobic residue is energetically favorable and entropy dominated on a methyl-terminated hydrophobic surface, energetically unfavorable and enthalpy dominated on a hydroxyl-terminated neutral hydrophilic surface, and very slightly favorable to unfavorable and enthalpy dominated on charged surfaces. These theoretical results provide a basis for understanding some of the fundamental effects governing protein adsorption to synthetic surfaces. This level of understanding is needed for the proactive design of surfaces to control protein adsorption and subsequent cellular response for both implant and tissue engineering applications. (C) 2002 Wiley Periodicals, Inc.