Thermodynamic perspectives on the molecular mechanisms providing protein adsorption resistance that include protein-surface interactions
Thermodynamic perspectives on the molecular mechanisms providing protein adsorption resistance that include protein-surface interactions
复制标题
DOI：
10.1002/jbm.a.30818
复制
发表时间：
2006-09-15
影响因子：
4.9
通讯作者：
Latour, Robert A.
中科院分区：
文献类型：
--
作者：
Latour, Robert A.
目前关于提供蛋白质吸附阻力的分子机制的理论主要集中在各种类型的表面束缚链的特性及其与水的相互作用，但往往忽略了它们与蛋白质的相互作用。因此，这些理论不能提供对蛋白质吸附阻力的完整解释。必须解决的真实的问题是，哪些特性使表面与水的相互作用比与蛋白质的相互作用更有利。为了解决这个问题，蛋白质吸附到表面束缚链的热力学处理和特定的分子水平的相互作用，有助于焓，熵，和自由能的变化，在蛋白质吸附过程中所涉及的解决。基于该分析，提出了两组独立可控的标准提供了在化学上有利于蛋白质吸附抗性的条件：（1）充分水合的长柔性表面束缚链，其堆积密度足够低以允许链移动性，同时仍然提供完全的表面覆盖，和（2）含有易于与水分子接触但不容易与蛋白质的氢键形成基团接触的可氢键合基团的表面束缚链。(c)2006 Wiley Periodicals，Inc.
Current theories regarding the molecular mechanisms that provide protein adsorption resistance primarily focus on the characteristics of various types of surface-tethered chains and their interactions with water but often neglect their interactions with the protein. Such theories thus do not provide a complete explanation for protein adsorption resistance. The real issue that must be addressed is which properties enable surfaces to interact with water more favorably than with proteins. To address this issue, a thermodynamic treatment of protein adsorption to surface-tethered chains is presented and specific molecular-level interactions are addressed that contribute to enthalpy, entropy, and free energy changes that are involved during protein adsorption processes. Based on this analysis, it is proposed that two independently controllable sets of criteria provide conditions that are thermodynamically favorable for protein adsorption resistance: (1) well-hydrated long flexible surface-tethered chains with packing density sufficiently low to allow chain mobility while still providing complete surface coverage, and (2) surface-tethered chains that contain hydrogen-bondable groups that are readily accessible to water molecules but not to the hydrogen bond-forming groups of a protein. (c) 2006 Wiley Periodicals, Inc.