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通过组装具有定制氨基酸序列的基因工程多肽来调整表面的刚度。

Tuning the Stiffness of Surfaces by Assembling Genetically Engineered Polypeptides with Tailored Amino Acid Sequence.

机构信息

3B's Research Group, I3Bs-Research Institute on Biomaterials, Biodegradables and Biomimetics , University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine , AvePark, Parque de Ciência e Tecnologia, Zona Industrial da Gandra , 4805-017 Barco, Guimarães , Portugal.

ICVS/3B's, PT Government Associated Laboratory , Braga/Guimarães , Portugal.

出版信息

Biomacromolecules. 2018 Aug 13;19(8):3401-3411. doi: 10.1021/acs.biomac.8b00723. Epub 2018 Jul 18.

DOI:10.1021/acs.biomac.8b00723
PMID:29969559
Abstract

We introduce elastin-like recombinamers (ELRs) as polypeptides with precise amino acid positioning to generate polypeptide coatings with tunable rigidity. Two ELRs are used: V84-ELR, a hydrophobic monoblock, and EI-ELR, an amphiphilic diblock. Both were modified with the amine-reactive tetrakis (hydroxymethyl) phosphonium chloride compound. We evaluated the affinity, conformation, and dissipative behavior of ELRs assembled on alkanethiol self-assembled coatings by quartz crystal microbalance with dissipation monitoring, multiparametric surface plasmon resonance, and atomic force microscopy. The thickness of the polypeptide coatings showcases the preferential affinity of ELRs to NH- and CH-terminated surfaces. We demonstrate that V84-ELR strongly bonded to the substrate and reorganizes into an extended and more hydrated layer as the adsorbed amount increases, whereas EI-ELR has a less dissipative behavior. The results suggest that ELR adsorption depends on the amino acid sequence and the substrate chemistry, ultimately influencing the stiffness of the polypeptide coatings.

摘要

我们引入弹性蛋白样重组体(ELR)作为具有精确氨基酸定位的多肽,以生成具有可调节刚性的多肽涂层。使用了两种 ELR:疏水单嵌段 V84-ELR 和两亲性双嵌段 EI-ELR。两者都用胺反应性四(羟甲基)鏻氯化物化合物进行了修饰。我们通过石英晶体微天平耗散监测、多参数表面等离子体共振和原子力显微镜评估了 ELR 在烷硫醇自组装涂层上组装的亲和力、构象和耗散行为。多肽涂层的厚度展示了 ELR 对 NH 和 CH 末端表面的优先亲和力。我们证明 V84-ELR 与基底强烈结合,并随着吸附量的增加重新组织成扩展且更水合的层,而 EI-ELR 的耗散行为较少。结果表明,ELR 的吸附取决于氨基酸序列和基底化学,最终影响多肽涂层的刚性。

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