PROTEIN SURFACE INTERACTIONS IN THE PRESENCE OF POLYETHYLENE OXIDE .1. SIMPLIFIED THEORY
PROTEIN SURFACE INTERACTIONS IN THE PRESENCE OF POLYETHYLENE OXIDE .1. SIMPLIFIED THEORY
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DOI：
10.1016/0021-9797(91)90043-8
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发表时间：
1991-03-01
影响因子：
9.9
通讯作者：
DEGENNES, PG
中科院分区：
文献类型：
--
作者：
JEON, SI;LEE, JH;DEGENNES, PG
从理论上研究了聚氧化乙烯（PEO）链末端附着在疏水固体基质上的抗蛋白质特性。考虑了空间排斥、货车范德华吸引和疏水相互作用自由能。结果与PEO的链长和表面密度有关。蛋白质通过扩散接近PEO表面，并通过水受到PEO表面和蛋白质之间的货车范德华吸引力的影响。蛋白质的进一步接近引发PEO链的压缩，其诱导空间排斥效应;另外的货车德瓦尔斯吸引力通过水溶剂化的PEO层在底物和蛋白质之间变得重要。货车德瓦耳斯组分随表面密度和末端连接的PEO链的链长的增加而减小。其他合成聚合物也进行了研究，表明蛋白质电阻特性与折射率有关，PEO具有最低的折射率的常见的水溶性合成聚合物。从文献数据PEO吸附到云母的渗透和弹性常数的空间排斥为终端连接的PEO估计为0.007和0.02，分别为。计算了PEO分子的空间排斥自由能以及空间排斥和疏水相互作用的结合自由能随PEO分子的表面密度和链长的变化关系。作为PEO的表面密度和链长的函数的自由能计算揭示，高表面密度和长链长度的末端连接的PEO应表现出最佳的蛋白质抗性，与PEO的高表面密度的实现比长链长度更重要。这些理论结果将有助于抗蛋白质吸附材料的设计和开发。
The protein resistance character of polyethylene oxide (PEO) chains terminally attached to a hydrophobic solid substrate is theoretically studied. Steric repulsion, van der Waals attraction, and hydrophobic interaction free energies are considered. The results are dependent on the chain length and surface density of PEO. The protein approaches the PEO surface by diffusion and is affected by the van der Waals attraction between the PEO surface and protein through water. Further approach of the protein initiates the compression of PEO chains, which induces a steric repulsion effect; an additional van der Waals attraction becomes important between the substrate and protein through the water solvated PEO layer. The van der Waals component with the substrate decreases with increasing surface density and chain length of terminally attached PEO chains. Other synthetic polymers were also studied, indicating that the protein resistance character is related to the refractive index, with PEO having the lowest refractive index of the common water-soluble synthetic polymers. The osmotic and elastic constants of steric repulsion for terminally attached PEO were estimated as ∼0.007 and 0.02, respectively, from literature data for PEO adsorbed to mica. The steric repulsion free energy and the combined steric repulsion and hydrophobic interaction free energies were calculated as a function of surface density and chain length of PEO. The free energy calculations as a function of surface density and chain length of PEO reveal that a high surface density and long chain length of terminally attached PEO should exhibit optimal protein resistance, with the attainment of high surface density of PEO being more important than long chain length. These theoretical results should be helpful in the design and development of materials resistant to protein adsorption.