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

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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.

Original language	English
Pages (from-to)	7700-7704
Journal	Organic and Biomolecular Chemistry
Volume	11
Issue number	44
DOIs	https://doi.org/10.1039/c3ob41837e
Publication status	Published - 1 Jan 2013

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title = "Triazole biotin: a tight-binding biotinidase-resistant conjugate",

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.",

author = "Germeroth, {Anne I.} and Hanna, {Jill R.} and Rehana Karim and Franziska Kundel and Jonathan Lowther and Neate, {Peter G. N.} and Blackburn, {Elizabeth A.} and Wear, {Martin A.} and Campopiano, {Dominic J.} and Hulme, {Alison N.}",

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doi = "10.1039/c3ob41837e",

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T1 - Triazole biotin: 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 - 2013/1/1

Y1 - 2013/1/1

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

SN - 1477-0520

VL - 11

SP - 7700

EP - 7704

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 44

ER -

Triazole biotin: a tight-binding biotinidase-resistant conjugate

Abstract

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