Albumin adsorption on Cibacron Blue F3G-A immobilized onto oligo(ethylene glycol)-terminated self-assembled monolayers
Albumin adsorption on Cibacron Blue F3G-A immobilized onto oligo(ethylene glycol)-terminated self-assembled monolayers
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DOI：
10.1023/a:1026394431100
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发表时间：
2003-11-01
影响因子：
3.7
通讯作者：
Barbosa, MA
中科院分区：
文献类型：
--
作者：
Martin, MCL;Naeemi, E;Barbosa, MA
自组装单分子层可以用特定配体针对某种蛋白质进行定制，同时防止其他蛋白质的非特异性吸附。 Cibacron Blue F3G-A（CB-硫醇）成功固定在四（乙二醇）封端的烷硫醇（CB-硫醇）上。使用具有不同正烷基链长度和功能末端基团（CH3-、OH-和四（乙二醇））的金上混合硫醇盐自组装单分子层研究人血清白蛋白（HSA）与固定化 Cibacron Blue F3G-A 的亲和力。使用 X 射线光电子能谱和水接触角测量对表面进行表征。使用 I-125 放射性标记的 HSA 评估白蛋白吸附以及吸附的白蛋白分子与溶液中其他白蛋白分子的交换性。还研究了白蛋白和纤维蛋白原对不同自组装单层 (SAM) 的竞争吸附。结果表明，在单层上掺入 CB-硫醇不会增加 SAM 上的 HSA 吸附和可逆性。然而，虽然未证明 HSA 对固定化 Cibacron Blue F3G-A 的特异性吸附，但 CB-硫醇的存在降低了纤维蛋白原与 OH 封端 SAM 的亲和力。 (C) 2003 年 Kluwer 学术出版社。
Self-assembled monolayers can be tailored with specific ligands to a certain protein and at the same time prevent the non-specific adsorption of other proteins. Cibacron Blue F3G-A (CB-thiol) was successfully immobilized onto tetra(ethylene glycol)-terminated alkanethiol (CB-thiol). The affinity of human serum albumin (HSA) to immobilized Cibacron Blue F3G-A was studied using mixed thiolate self-assembled monolayers on gold with different n-alkyl chain lengths and functional terminal groups (CH3-; OH- and tetra(ethylene glycol)).Surfaces were characterized using X-ray photoelectron spectroscopy and water contact angle measurements. Albumin adsorption and exchangeability of the adsorbed albumin molecules with other albumin molecules in solution were evaluated using I-125-radiolabeled HSA. Competitive adsorption between albumin and fibrinogen to the different self-assembled monolayers (SAMs) was also investigated. Results showed that the incorporation of CB-thiol on the monolayers does not increase the HSA adsorption and reversibility on the SAMs. However, although specific adsorption of HSA to the immobilized Cibacron Blue F3G-A was not demonstrated, the presence of CB-thiol decreases the affinity of fibrinogen to the OH-terminated SAMs. (C) 2003 Kluwer Academic Publishers.