抗生素蜘蛛丝：利用“点击”化学对重组蜘蛛丝进行定点功能化。
Antibiotic Spider Silk: Site-Specific Functionalization of Recombinant Spider Silk Using "Click" Chemistry.
机构信息
School of Chemistry, Centre for Biomolecular Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.
School of Life Sciences, University of Nottingham, Nottingham, NG7 2RD, UK.
出版信息
Adv Mater. 2017 Mar;29(10). doi: 10.1002/adma.201604245. Epub 2016 Dec 28.
In a new, versatile approach to fun-ction-alizing recombinant spider silk, L-azidohomoalanine is introduced residue-specifically in the minispidroin protein 4RepCT through expression in an E. coli methionine auxotroph. Both fluorophores and the antibiotic levofloxacin are attached to this bio-orthogonal amino acid using copper-catalyzed click chemistry, either before or after the silk fibers are self-assembled.
在一种新的、多功能的方法中，通过在大肠杆菌蛋氨酸营养缺陷型中表达，将 L-叠氮高丙氨酸残基特异性地引入到 minispidroin 蛋白 4RepCT 中，从而实现重组蜘蛛丝的功能化。使用铜催化的点击化学，无论是在纤维自组装之前还是之后，都可以将荧光团和抗生素左氧氟沙星连接到这种生物正交氨基酸上。
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