Self-assembly of bivalent protein-binding agents based on oligonucleotide-linked organic fragments

K. Ingrid Sprinz; Debarati M. Tagore; Andrew D. Hamilton

doi:10.1016/j.bmcl.2005.05.094

Self-assembly of bivalent protein-binding agents based on oligonucleotide-linked organic fragments

K. Ingrid Sprinz, Debarati M. Tagore, Andrew D. Hamilton

Chemistry

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

Abstract

A library of bidentate fragments linked through an oligonucleotide duplex was tested for binding to streptavidin. When one fragment was biotin, only biotin-containing duplexes were selected by streptavidin but when heated above the melting temperature, only bidentate biotin ligands were obtained. Thermal denaturation experiments showed that the melting temperature, thus stability, of the monodentate versus bidentate binding ligand increased from 59 to 71°C in the presence of streptavidin. Substituting biotin with 2-iminobiotin led to the exclusion of all other duplexes by the bidentate iminobiotin duplex in binding streptavidin.

Original language	English (US)
Pages (from-to)	3908-3911
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	15
Issue number	17
DOIs	https://doi.org/10.1016/j.bmcl.2005.05.094
State	Published - Sep 1 2005

Keywords

Bidentate
Combinatorial library
Monodentate
Thermal denaturation

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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10.1016/j.bmcl.2005.05.094

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title = "Self-assembly of bivalent protein-binding agents based on oligonucleotide-linked organic fragments",

abstract = "A library of bidentate fragments linked through an oligonucleotide duplex was tested for binding to streptavidin. When one fragment was biotin, only biotin-containing duplexes were selected by streptavidin but when heated above the melting temperature, only bidentate biotin ligands were obtained. Thermal denaturation experiments showed that the melting temperature, thus stability, of the monodentate versus bidentate binding ligand increased from 59 to 71°C in the presence of streptavidin. Substituting biotin with 2-iminobiotin led to the exclusion of all other duplexes by the bidentate iminobiotin duplex in binding streptavidin.",

keywords = "Bidentate, Combinatorial library, Monodentate, Thermal denaturation",

author = "Sprinz, {K. Ingrid} and Tagore, {Debarati M.} and Hamilton, {Andrew D.}",

note = "Funding Information: This work was supported in part by the National Institutes of Health (GM 35208). Our special thanks to Prof. Peter Moore for use of his radioactive laboratory and Prof. Donald Crothers for use of his Cary I UV–vis spectrophotometer. We would also like to thank Vishwanath Jogini for generating Figure 2 B. ",

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doi = "10.1016/j.bmcl.2005.05.094",

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T1 - Self-assembly of bivalent protein-binding agents based on oligonucleotide-linked organic fragments

AU - Sprinz, K. Ingrid

AU - Tagore, Debarati M.

AU - Hamilton, Andrew D.

N1 - Funding Information: This work was supported in part by the National Institutes of Health (GM 35208). Our special thanks to Prof. Peter Moore for use of his radioactive laboratory and Prof. Donald Crothers for use of his Cary I UV–vis spectrophotometer. We would also like to thank Vishwanath Jogini for generating Figure 2 B.

PY - 2005/9/1

Y1 - 2005/9/1

N2 - A library of bidentate fragments linked through an oligonucleotide duplex was tested for binding to streptavidin. When one fragment was biotin, only biotin-containing duplexes were selected by streptavidin but when heated above the melting temperature, only bidentate biotin ligands were obtained. Thermal denaturation experiments showed that the melting temperature, thus stability, of the monodentate versus bidentate binding ligand increased from 59 to 71°C in the presence of streptavidin. Substituting biotin with 2-iminobiotin led to the exclusion of all other duplexes by the bidentate iminobiotin duplex in binding streptavidin.

AB - A library of bidentate fragments linked through an oligonucleotide duplex was tested for binding to streptavidin. When one fragment was biotin, only biotin-containing duplexes were selected by streptavidin but when heated above the melting temperature, only bidentate biotin ligands were obtained. Thermal denaturation experiments showed that the melting temperature, thus stability, of the monodentate versus bidentate binding ligand increased from 59 to 71°C in the presence of streptavidin. Substituting biotin with 2-iminobiotin led to the exclusion of all other duplexes by the bidentate iminobiotin duplex in binding streptavidin.

KW - Bidentate

KW - Combinatorial library

KW - Monodentate

KW - Thermal denaturation

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Self-assembly of bivalent protein-binding agents based on oligonucleotide-linked organic fragments

Abstract

Keywords

ASJC Scopus subject areas

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