Triazole biotin: a tight-binding biotinidase-resistant conjugate

Anne I Germeroth; Jill R Hanna; Rehana Karim; Franziska Kundel; Jonathan Lowther; Peter G N Neate; Elizabeth A Blackburn; Martin A Wear; Dominic J Campopiano; Alison N Hulme

doi:10.1039/c3ob41837e

Triazole biotin: a tight-binding biotinidase-resistant conjugate

Anne I Germeroth, Jill R Hanna, Rehana Karim, Franziska Kundel, Jonathan Lowther, Peter G N Neate, Elizabeth A Blackburn, Martin A Wear, Dominic J Campopiano, Alison N Hulme

Research output: Contribution to journal › Article › peer-review

Abstract

The natural amide bond found in all biotinylated proteins has been replaced with a triazole through CuAAC reaction of an alkynyl biotin derivative. The resultant triazole-linked adducts are shown to be highly resistant to the ubiquitous hydrolytic enzyme biotinidase and to bind avidin with dissociation constants in the low pM range. Application of this strategy to the production of a series of biotinidase-resistant biotin-Gd-DOTA contrast agents is demonstrated.

Original language	English
Pages (from-to)	7700-7704
Number of pages	5
Journal	Organic & Biomolecular chemistry
Volume	11
Issue number	44
DOIs	https://doi.org/10.1039/c3ob41837e
Publication status	Published - 10 Oct 2013

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abstract = "The natural amide bond found in all biotinylated proteins has been replaced with a triazole through CuAAC reaction of an alkynyl biotin derivative. The resultant triazole-linked adducts are shown to be highly resistant to the ubiquitous hydrolytic enzyme biotinidase and to bind avidin with dissociation constants in the low pM range. Application of this strategy to the production of a series of biotinidase-resistant biotin-Gd-DOTA contrast agents is demonstrated.",

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T2 - a tight-binding biotinidase-resistant conjugate

AU - Germeroth, Anne I

AU - Hanna, Jill R

AU - Karim, Rehana

AU - Kundel, Franziska

AU - Lowther, Jonathan

AU - Neate, Peter G N

AU - Blackburn, Elizabeth A

AU - Wear, Martin A

AU - Campopiano, Dominic J

AU - Hulme, Alison N

PY - 2013/10/10

Y1 - 2013/10/10

N2 - The natural amide bond found in all biotinylated proteins has been replaced with a triazole through CuAAC reaction of an alkynyl biotin derivative. The resultant triazole-linked adducts are shown to be highly resistant to the ubiquitous hydrolytic enzyme biotinidase and to bind avidin with dissociation constants in the low pM range. Application of this strategy to the production of a series of biotinidase-resistant biotin-Gd-DOTA contrast agents is demonstrated.

AB - The natural amide bond found in all biotinylated proteins has been replaced with a triazole through CuAAC reaction of an alkynyl biotin derivative. The resultant triazole-linked adducts are shown to be highly resistant to the ubiquitous hydrolytic enzyme biotinidase and to bind avidin with dissociation constants in the low pM range. Application of this strategy to the production of a series of biotinidase-resistant biotin-Gd-DOTA contrast agents is demonstrated.

U2 - 10.1039/c3ob41837e

DO - 10.1039/c3ob41837e

M3 - Article

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SN - 1477-0520

VL - 11

SP - 7700

EP - 7704

JO - Organic & Biomolecular chemistry

JF - Organic & Biomolecular chemistry

IS - 44

ER -

Triazole biotin: a tight-binding biotinidase-resistant conjugate

Abstract

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