Sequence-specific crosslinking of electrospun, elastin-like protein preserves bioactivity and native-like mechanics.
Sequence-specific crosslinking of electrospun, elastin-like protein preserves bioactivity and native-like mechanics.
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DOI：
10.1002/adhm.201200115
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发表时间：
2013-01
影响因子：
10
通讯作者：
Heilshorn, Sarah C.
中科院分区：
文献类型：
--
作者：
Benitez, Patrick L.;Sweet, Jeffrey A.;Fink, Helen;Chennazhi, Krishna P.;Nair, Shantikumar V.;Enejder, Annika;Heilshorn, Sarah C.
工程化细胞外基质（eECM）广泛地模拟体内微环境，同时提供若干可调参数，为组织工程应用提供生理上但精细控制的基质细胞信号。理想的eECM具有纳米纤维结构，组织样力学和特定的生物活性配体，其中每一个都应该在生理范围内可调节以用于所需的应用。为了满足这一需求，将重组弹性蛋白样蛋白（ELP）的多变量可调家族从水溶液电纺成可植入的纳米纤维织物。虽然重组蛋白的电纺不是一个新的想法，但以前的努力依赖于与合成聚合物共混或与非特异性固定剂交联以获得稳定的纤维基质。这些过程降低了蛋白质纳米纤维的生理逼真性和特异性，从而破坏了基于蛋白质的生物材料的目的。在这里，通过分析ELP的热力学行为，我们设计了一种新的，序列特异性的，连续的过程，包括气相引发和交联的水溶液完成（图1a）。序列特异性交联（a）通过纳米纤维保留了沿着蛋白质骨架表达的精氨酸-甘氨酸-天冬氨酸（RGD）配体，并且（B）为细胞-基质相互作用提供了稳定的纳米拓扑学和天然样机制。单根光纤呈带状（厚度为190±60 nm），宽度可调（1.2-1.8 μ m
Engineered extracellular matrices (eECMs) that broadly mimic the in vivo microenvironment while offering several tunable parameters provide physiological yet finely controlled matrix-cell signals for tissue engineering applications. The ideal eECM has nanofibrous architecture, tissue-like mechanics, and specific bioactive ligands, each of which should be adjustable over a physiological range for desired applications. To meet this need, a multivariately tunable family of recombinant elastin-like proteins (ELPs) is electrospun into an implantable, nanofibrous fabric from aqueous solution. Although electrospinning of recombinant proteins is not a new idea, previous efforts have relied on blending with synthetic polymers or crosslinking with non-specific fixatives to achieve stable fibrous matrices. These processes decrease the physiological verisimilitude and specificity of protein nanofibers, thus defeating the purpose of protein-based biomaterials. Here, by analyzing ELP's thermodynamic behavior, we devise a novel, sequence-specific, sequential process comprised of vapor-phase initiation and aqueous completion of crosslinks (Figure 1 a). Sequence-specific crosslinking (a) preserves arginine-glycine-aspartic acid (RGD) ligands, expressed along the protein's backbone, through nanofabrication and (b) provides stable nanotopology and native-like mechanics for cell-matrix interactions. Individual fibers are ribbon-like (thickness of 190±60 nm) with tunable widths (1.2–1.8 μ
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影响因子：
6.2
作者：
Qiu, Weiguo;Huang, Yiding;Teng, Weibing;Cohn, Celine M.;Cappello, Joseph;Wu, Xiaoyi
通讯作者：
Wu, Xiaoyi
影响因子：
14
作者：
Rnjak-Kovacina, Jelena;Wise, Steven G.;Weiss, Anthony S.
通讯作者：
Weiss, Anthony S.
影响因子：
5.5
作者：
Lee, J;Macosko, CW;Urry, DW
通讯作者：
Urry, DW
影响因子：
6.2
作者：
Reguera, Javier;Urry, Dan W.;Rodriguez-Cabello, J. Carlos
通讯作者：
Rodriguez-Cabello, J. Carlos
DOI：
10.1083/jcb.200405004
发表时间：
2004-09-13
期刊：
The Journal of cell biology
影响因子：
--
作者：
Engler AJ;Griffin MA;Sen S;Bönnemann CG;Sweeney HL;Discher DE
通讯作者：
Discher DE