Zwitterionic SAMs that resist nonspecific adsorption of protein from aqueous buffer
Zwitterionic SAMs that resist nonspecific adsorption of protein from aqueous buffer
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DOI：
10.1021/la0015258
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发表时间：
2001-05-01
期刊：
影响因子：
3.9
通讯作者：
Whitesides, GM
中科院分区：
文献类型：
--
作者：
Holmlin, RE;Chen, XX;Whitesides, GM
本文介绍了使用表面等离子体共振光谱和自组装单分子膜（SAMs）的烷硫醇在金，以评估在不同的带电基团的组合，以抵抗非特异性吸附的蛋白质从水性缓冲液的表面终止的能力。由三甲基铵基封端的硫醇和磺酸基封端的硫醇以1：1组合形成的混合自组装膜吸附了不到1%的两种具有不同特征的蛋白质单层：纤维蛋白原和溶菌酶。单组分自组装膜形成的硫醇终止在一个带正电荷的部分和一个带负电荷的部分相结合的基团也能够抵抗蛋白质的吸附。单组分自组装膜呈现单电荷吸附几乎整个单层的蛋白质。吸附到混合两性离子自组装膜的蛋白质的量不依赖于蛋白质溶解于其中的缓冲液的离子强度或pH。吸附到单组分两性离子自组装膜的蛋白质的量随着缓冲液的离子强度的降低而增加;它也随着缓冲液的pH值的增加（在恒定的离子强度下）而降低。单组分两性离子自组装膜由以N终止的硫醇组成，N-二甲基氨基丙烷-1-磺酸（-N+（CH 3）（2）CH 2CH 2CH 2SO 3-）基团在生理离子强度和pH下抵抗纤维蛋白原和溶菌酶从缓冲液中的吸附方面比由以磷酸2-三甲基氨基乙酯（-OP（O）（2）-OCH 2CH 2N+（CH3）（3））。这些两性离子自组装膜中的几种可与抗蛋白质非特异性吸附的最佳已知系统相媲美。
This paper describes the use of surface plasmon resonance spectroscopy and self-assembled monolayers (SAMs) of alkanethiols on gold to evaluate the ability of surfaces terminating in different combinations of charged groups to resist the nonspecific adsorption of proteins from aqueous buffer. Mixed SAMs formed from a 1:1 combination of a thiol terminated in a trimethylammonium group and a thiol terminated in a sulfonate group adsorbed less than 1% of a monolayer of two proteins with different characteristics: fibrinogen and lysozyme. Single-component SAMs formed from thiols terminating in groups combining a positively charged moiety and a negatively charged moiety were also capable of resisting the adsorption of proteins. Single-component SAMs presenting single charges adsorbed nearly a full monolayer of protein. The amount of protein that adsorbed to mixed zwitterionic SAMs did not depend on the ionic strength or the pH of the buffer in which the protein was dissolved. The amount of protein that adsorbed to single-component zwitterionic SAMs increased as the ionic strength of the buffer decreased; it also decreased as the pH of the buffer increased (at constant ionic strength). Single-component zwitterionic SAMs composed of thiols terminating in N,N-dimethyl-amino-propane-1-sulfonic acid (-N+(CH3)(2)CH2CH2CH2SO3-) groups were substantially more effective at resisting adsorption of fibrinogen and lysozyme from buffer at physiological ionic strength and pH than single-component zwitterionic SAMs composed of thiols terminating in phosphoric acid 2-trimethylamino-ethyl ester (-OP(O)(2)-OCH2CH2N+(CH3)(3)). Several of these zwitterionic SAMs were comparable to the best known systems for resisting nonspecific adsorption of protein.