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Trends in Biotechnology:蛋白质之间不可牢破的键

2015-01-04 14:26  
内容快照:

Trends in Biotechnology封面:蛋白质之间不可牢破的键

摘要 : 在2014年10月Trends in Biotechnology期刊封面文章中,Veggiani和同事探讨了SpyTag和SpyCatcher之间的不可逆的蛋白质 - 蛋白质相互作用,以及由SpyLigase催化不可逆的蛋白质 - 蛋白质相互作用,以及这些类型的键的各种新应用。

蛋白质工程的下一步将是操纵多肽和蛋白质之间的共价相互作用。控制异肽键的形成可为这个任务提供适当的特异性和通用性。

Superglue from bacteria: unbreakable bridges for protein nanotechnology.Gianluca Veggiani, Bijan Zakeri, Mark Howarth.DOI:http://dx.doi.org/10.1016/j.tibtech.2014.08.001

Highlights

Strong links between proteins are important in many areas of biotechnology.

SpyTag is a peptide forming a spontaneous isopeptide bond to the protein SpyCatcher.

Each component can be fused genetically and reacts under diverse conditions.

Uses include resisting force, targeting nanoparticles, and enhancing enzyme stability.

Biotechnology is often limited by weak interactions. We suggest that an ideal interaction between proteins would be covalent, specific, require addition of only a peptide tag to the protein of interest, and form under a wide range of conditions. Here we summarize peptide tags that are able to form spontaneous amide bonds, based on harnessing reactions of adhesion proteins from the bacterium Streptococcus pyogenes. These include the irreversible peptide–protein interaction of SpyTag with SpyCatcher, as well as irreversible peptide–peptide interactions via SpyLigase. We describe existing applications, including polymerization to enhance cancer cell capture, assembly of living biomaterial, access to diverse protein shapes, and improved enzyme resilience. We also indicate future opportunities for resisting biological force and extending the scope of protein nanotechnology.


Keywords:
protein engineering, nanobiotechnology, mechanobiology, synthetic biology, supramolecular assembly, biomimetic

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