3 years ago

Enzymatic Installation of Functional Molecules on Amyloid-Based Polymers

Enzymatic Installation of Functional Molecules on Amyloid-Based Polymers
Masafumi Sakono, Tatsuki Ohshima
We produced a functional polymer whose framework comprised transthyretin (TTR) amyloid fibrils. In order to immobilize functional molecules onto the amyloid fibrils, transpeptidase sortase A (srtA), which catalyzes the covalent binding of LPXTG with polyglycine, was employed. After the preparation of the amyloid fibril of LPETGG-tagged TTR, immobilization of Gly5-fused GFP on the amyloid fibrils by srtA-mediated transpeptidation was carried out. SrtA recognized the amyloid fibrils consisting of an LPETGG-tagged TTR variant (L55P) as a good substrate, resulting in successful preparation of a GFP-immobilized amyloid. Intriguingly, the replacement of GFP with Gly5-fused luciferase was confirmed when the GFP-immobilized amyloids were mixed with Gly5-luciferase in the presence of srtA. Thus, it was found that functional molecules covalently immobilized on amyloid could be detached and substituted with other tagged molecules by using srtA.

Publisher URL: http://dx.doi.org/10.1021/acs.bioconjchem.7b00479

DOI: 10.1021/acs.bioconjchem.7b00479

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