Denis Frédéric A, Pallandre Antoine, Nysten Bernard, Jonas Alain M, Dupont-Gillain Christine C
Unité de Chimie des Interfaces, Université Catholique de Louvain, Croix du Sud 2/18, 1348 Louvain-la-Neuve, Belgium.
Small. 2005 Oct;1(10):984-91. doi: 10.1002/smll.200500116.
Collagen, a protein widely used to control cell-material interactions, is known to self-assemble in solution. Supramolecular structures also form on material surfaces following collagen adsorption. Herein, we report the use of anisotropic, flat, surface chemical nanopatterns, which consist of alkyl-terminated tracks drawn in an oligo(ethylene glycol)-terminated matrix, to direct collagen adsorption. As revealed by atomic force microscopy, the spontaneous collagen adsorption performed on such patterned substrates results in the accumulation of collagen on the hydrophobic tracks. Moreover, the width of the tracks (30-90 nm), which is much smaller than the length of the collagen molecule (approximately 300 nm), is the origin of preferential alignment of the molecules and of their assembly into continuous bundles of adsorbed collagen. This chemical guidance effect due to self-confinement of proteins upon adsorption may bring novel and valuable applications, specifically in biomaterials science and cell growth control.
胶原蛋白是一种广泛用于控制细胞与材料相互作用的蛋白质，已知其在溶液中会自组装。胶原蛋白吸附后，超分子结构也会在材料表面形成。在此，我们报告了使用由在以寡聚（乙二醇）为末端的基质中绘制的烷基末端轨道组成的各向异性、平坦的表面化学纳米图案来引导胶原蛋白吸附。如原子力显微镜所揭示的，在这种图案化底物上进行的自发胶原蛋白吸附导致胶原蛋白在疏水轨道上积累。此外，轨道宽度（30 - 90纳米）远小于胶原蛋白分子的长度（约300纳米），这是分子优先排列及其组装成连续吸附胶原蛋白束的原因。这种由于蛋白质吸附时的自限制而产生的化学引导效应可能带来新颖且有价值的应用，特别是在生物材料科学和细胞生长控制方面。
