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与京尼平及吡咯喹啉醌交联的弹性蛋白基多肽的微观结构和拉伸性能

Microstructural and tensile properties of elastin-based polypeptides crosslinked with genipin and pyrroloquinoline quinone.

作者信息

Vieth S, Bellingham C M, Keeley F W, Hodge S M, Rousseau D

机构信息

School of Chemical Engineering, Ryerson University, Toronto, Ontario, Canada.

出版信息

Biopolymers. 2007 Feb 15;85(3):199-206. doi: 10.1002/bip.20619.

DOI:10.1002/bip.20619
PMID:17066474
Abstract

Elastin is an elastomeric, self-assembling extracellular matrix protein with potential for use in biomaterials applications. Here, we compare the microstructural and tensile properties of the elastin-based recombinant polypeptide (EP) EP20-244 crosslinked with either genipin (GP) or pyrroloquinoline quinone (PQQ). Recombinant EP-based sheets were produced via coacervation and subsequent crosslinking. The micron-scale topography of the GP-crosslinked sheets examined with atomic force microscopy revealed the presence of extensive mottling compared with that of the PQQ-crosslinked sheets, which were comparatively smoother. Confocal microscopy showed that the subsurface porosity in the GP-crosslinked sheets was much more open. GP-crosslinked EP-based sheets exhibited significantly greater tensile strength (P < or = 0.05). Mechanistically, GP appears to yield a higher crosslink density than PQQ, likely due to its capacity to form short-range and long-range crosslinks. In conclusion, GP is able to strongly modulate the microstructural and mechanical properties of elastin-based polypeptide biomaterials forming membranes with mechanical properties similar to native insoluble elastin.

摘要

弹性蛋白是一种具有弹性、能自我组装的细胞外基质蛋白,有用于生物材料应用的潜力。在此,我们比较了用京尼平(GP)或吡咯喹啉醌(PQQ)交联的基于弹性蛋白的重组多肽(EP)EP20 - 244的微观结构和拉伸性能。基于重组EP的片材通过凝聚及随后的交联制备而成。用原子力显微镜检查的GP交联片材的微米级形貌显示,与相对更光滑的PQQ交联片材相比,存在大量斑点。共聚焦显微镜显示,GP交联片材的亚表面孔隙更开放。基于GP交联的EP片材表现出显著更高的拉伸强度(P≤0.05)。从机制上讲,GP似乎比PQQ产生更高的交联密度,这可能是由于其形成短程和长程交联的能力。总之,GP能够强烈调节基于弹性蛋白的多肽生物材料的微观结构和力学性能,形成具有与天然不溶性弹性蛋白相似力学性能的膜。

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