Perelman Loren A, Schwartz Michael P, Wohlrab Aaron M, Vannieuwenhze Michael S, Sailor Michael J
Materials Science and Engineering Program, University of California, San Diego, 9500 Gilman Drive, San Diego, CA 92093, USA.
Physica Status Solidi A Appl Res. 2007 May;204(5):1394-1398. doi: 10.1002/pssa.200674360.
A simple strategy for linking biomolecules to porous Si surfaces and detecting peptide/drug binding is described. Porous Si is prepared using an electrochemical etch and then thermally oxidized by heating in ambient atmosphere. Bovine serum albumin (BSA) is then non-covalently adsorbed to the inner pore walls of the porous Si oxide (PSiO(2)) matrix. The BSA layer is used as a linker for covalent attachment of the peptide Ac-L-Lysine-D-Alanine-D-Alanine (KAA) using published bioconjugation chemistry. BSA-coated surfaces functionalized with KAA display specificity for the glycopeptide vancomycin while resisting adsorption of non-specific reagents. While the biomolecule attachment strategy reported here is used to bind peptides, the scheme can be generalized to the linking of any primary amine-containing molecule to PSiO(2) surfaces.
本文描述了一种将生物分子连接到多孔硅表面并检测肽/药物结合的简单策略。多孔硅通过电化学蚀刻制备,然后在环境气氛中加热进行热氧化。接着,牛血清白蛋白(BSA)非共价吸附到多孔氧化硅(PSiO₂)基质的内孔壁上。利用已发表的生物共轭化学方法,将BSA层用作肽Ac-L-赖氨酸-D-丙氨酸-D-丙氨酸(KAA)共价连接的连接体。用KAA功能化的BSA包被表面对糖肽万古霉素具有特异性,同时能抵抗非特异性试剂的吸附。虽然此处报道的生物分子连接策略用于结合肽,但该方案可推广到将任何含伯胺的分子连接到PSiO₂表面。