Nanoscale clustering of RGD peptides at surfaces using comb polymers. 1. Synthesis and characterization of comb thin films
Nanoscale clustering of RGD peptides at surfaces using comb polymers. 1. Synthesis and characterization of comb thin films
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DOI：
10.1021/bm005584b
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发表时间：
2001-03-01
影响因子：
6.2
通讯作者：
Griffith, LG
中科院分区：
文献类型：
--
作者：
Irvine, DJ;Mayes, AM;Griffith, LG
理论和实验研究进行了阐明的两亲性梳状聚合物薄膜的结构和性能呈现纳米簇的Arg-Gly-Asp（RGD）肽的生物材料上的细胞粘附控制。合成了由聚（甲基丙烯酸甲酯）主链和短聚（环氧乙烷）侧链组成的梳状物，并将肽系在侧链末端以产生纳米级肽簇。在薄膜中，含有大于或等于30重量%的6至9个单元PEO侧链的梳形聚合物在7.5%血清存在下在24小时内完全抵抗模型成纤维细胞系的粘附。这些相同的聚合物修饰的RGD肽引起可调的细胞粘附时，以不同的比例与未修饰的梳子混合。梳形聚合物薄膜和水之间的界面的自洽场晶格模型预测梳形聚合物的顶部分子层的组织与平行于界面的骨干取向在准二维限制和亲水性侧链延伸到溶液中的刷状层。准2D配置的这张图片与所观察到的梳状膜在水中的表面性质以及使用配体簇的荧光纳米球标记的混合梳状表面上的RGD簇密度的测量是一致的。
Theoretical and experimental studies were conducted to elucidate the structure and properties of amphiphilic comb polymer thin films presenting nanoscale clusters of Arg-Gly-Asp (RGD) peptides for control of cell adhesion on biomaterials. Combs comprised of a poly(methyl methacrylate) backbone and short poly(ethylene oxide) side chains were synthesized, and peptides were tethered to the side chain ends to create nanoscale peptide clusters. In thin films, comb polymers containing greater than or equal to 30 wt % six to nine unit PEO side chains completely resisted adhesion of a model fibroblast cell line in the presence of 7.5% serum over 24 h. These same polymers modified with RGD peptides elicited tunable cell adhesion when mixed with unmodified combs in varying proportion. A self-consistent field lattice model of the interface between comb polymer films and water predicts an organization of the top molecular layer of comb polymer with the backbone oriented parallel to the interface in quasi-two-dimensional confinement and hydrophilic side chains extended in a brushlike layer into solution. This picture of a quasi-2D configuration is consistent with the observed surface properties of comb films in water as well as measurements of the RGD cluster density on mixed comb surfaces using fluorescent nanosphere labeling of ligand clusters.