Solvent effect and time-dependent behavior of C-terminus-cysteine-modified cecropin P1 chemically immobilized on a polymer surface.
Solvent effect and time-dependent behavior of C-terminus-cysteine-modified cecropin P1 chemically immobilized on a polymer surface.
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DOI：
10.1021/la200388y
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发表时间：
2011-06-07
期刊：
影响因子：
--
通讯作者：
Chen Z
中科院分区：
文献类型：
--
作者：
Han X;Soblosky L;Slutsky M;Mello CM;Chen Z
利用和频(SFG)振动光谱研究了多肽在聚合物表面的固定化与时间和多肽构象的关系。生物分子的表面固定化在生物传感器、抗菌材料、生物燃料电池、纳米制造和多功能材料等方面具有重要的应用价值。以C端半胱氨酸修饰的天蚕素P1(CP1c)为模型，实时研究了固定化过程中随时间变化的行为。此外，利用磷酸二氢钾缓冲液(PB)和PB与三氟乙醇的混合物考察了多肽二级结构对CP1c固定化聚苯乙烯马来酰亚胺(PS-MA)的影响。利用偏振SFG光谱确定了固定化CP1c在PS-MA上的取向。研究发现，多肽溶液浓度、溶剂组成和固定化前的组装状态(单体和二聚体)都会影响CP1c在PS-MA表面的取向。讨论了界面多肽取向与固定化条件之间的具体关系。
Sum frequency generation (SFG) vibrational spectroscopy has been applied to investigate peptide immobilization to a polymer surface as a function of time and peptide conformation. Surface immobilization of biological molecules is important in many applications such as biosensors, antimicrobial materials, bio-based fuel cells, nanofabrication, and multi-functional materials. Using C-terminus cysteine modified cecropin P1 (CP1c) as a model, we investigated the time-dependent immobilization behavior in situ in real time. In addition, potassium phosphate buffer (PB) and mixtures of PB and trifluoroethanol were utilized to examine the effect of peptide secondary structure on CP1c immobilization to polystyrene maleimide (PS-MA). The orientation of immobilized CP1c on PS-MA was determined using polarized SFG spectra. It was found that the peptide solution concentration, solvent composition, and assembly state (monomer vs. dimer) prior to immobilization all influence the orientation of CP1c on a PS-MA surface. The detailed relationship between interfacial peptide orientation and these immobilization conditions is discussed.
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