首页|Synthesis of globotriose-modified peptides for the preparation of a colorimetric biosensor to detect Shiga toxins
Synthesis of globotriose-modified peptides for the preparation of a colorimetric biosensor to detect Shiga toxins
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NSTL
Elsevier
Globotriose (Gal-alpha 1, 4-Gal-beta 1, 4-Glc) is involved in binding with Shiga toxins (Stxs) produced by Shigella dys-enteriae and certain pathogenic Escherichia coli strains which could cause severe gastroenteritis and hemolytic uremic syndrome (HUS). Thus, this trisaccharide group and its derivatives provide potentials in the development of carbohydrate-based diagnostic and therapeutic reagents against bacterial infection. Instead of the tedious chemical synthesis of globotriose or its glycoconjugates, we reported a multi-step (step-wise) enzymatic synthesis system containing glucosyltransferase (ApNGT, E.C. 4.3.3.5), beta-1, 4-galactosyltransferase (LgtB, E.C. 2.4.1.22) and alpha-1, 4-galactosyltransferase (LgtC, E.C. 2.4.1.44) to produce globotriose-containing glycopeptides. In addi-tion, based on the specific binding between Stxs and globotriose, a cost-efficient, convenient, ultra-sensitive and specific colorimetric biosensor was further constructed to detect Stxs using glycoconjugated Au@Fe-TFPA-COP (globotriose@Au@Fe-TFPA-COP) as a nanoenzyme catalyst. We estimate that this method conveniently applied in the detection of Stx-producing bacteria and associated infectious diseases.
Multi -step enzymatic synthesisGlobotrioseGlycopeptideShiga toxinGlyconanoparticleEFFICIENT CHEMOENZYMATIC SYNTHESISFUNCTIONAL TRANSFERGOLD NANOPARTICLESGLYCOSYLATIONBINDING
NSTL
Elsevier
