Adsorption of Cu (II) ions from aqueous solution using pyridine-2,6- Dicarboxylic acid cross-linked
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Abstract
The potential applications of recombinant bacterial collagen- like proteins are limited by lacking high order structures to form biomaterials. To improve the self-assembly ability of collagen- like proteins, we have designed collagen-like engineered proteins flanked by N- and C-terminal (PPG)10 sequences. Upon expression in E. coli, these designs self-assembled into axial D- periodic fibers with spacing matching the length of the bacterial collagen domain. Computational analysis of self-assembly has given insight into the mechanism behind the banded fiber morphology. The interactions between collagen designs and cultured fibroblasts are being studied to determine how fiber morphology affects cell structure and viability. This study provides a design strategy for the production of collagen proteins with functional sequences and tunable morphology for biomimetic materials in tissue engineering applications. The collagen proteins flanked by N- and C-terminal (PPG)10 sequence can be successfully expressed in E.coli and self- assembled into D-periodic fibers regardless of collagen-like domain. Through regulated the length of the collagen domain, we can change the length of D-periodicity
