Molecular interactions in the insulin-like growth factor (IGF) axis: a surface plasmon resonance (SPR) based biosensor study

G.J. Allan, J. Beattie, J.H. Shand, M. Szymanowska, D.J. Flint

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

This review describes a comprehensive analysis of a surface plasmon resonance (SPR)-based biosensor study of molecular interactions in the insulin-like growth factor (IGF) molecular axis. In this study, we focus on the interaction between the polypeptide growth factors IGF-I and IGF-II with six soluble IGF binding proteins (IGFBP 1-6), which occur naturally in various biological fluids. We have describe the conditions required for the accurate determination of kinetic rate constants for these interactions and highlight the experimental and theoretical pitfalls, which may be encountered in the early stages of such a study. We focus on IGFBP-5 and describe a site-directed mutagenesis study, which examines the contribution of various residues in the protein to high affinity interaction with IGF-I and -II. We analyse the interaction of IGFBP-5 (and IGFBP-3) with heparin and other biomolecules and describe experiments, which were designed to monitor multi-protein complex formation in this molecular axis.
LanguageEnglish
Pages221-236
Number of pages15
JournalMolecular and Cellular Biochemistry
Volume307
Issue number1-2
DOIs
Publication statusPublished - 2008

Fingerprint

Insulin-Like Growth Factor Binding Protein 5
Insulin-Like Growth Factor Binding Protein 1
Insulin-Like Growth Factor II
Surface Plasmon Resonance
Molecular interactions
Surface plasmon resonance
Biosensing Techniques
Somatomedins
Insulin-Like Growth Factor I
Biosensors
Insulin-Like Growth Factor Binding Protein 6
Insulin-Like Growth Factor Binding Proteins
Mutagenesis
Insulin-Like Growth Factor Binding Protein 3
Biomolecules
Site-Directed Mutagenesis
Heparin
Rate constants
Intercellular Signaling Peptides and Proteins
Proteins

Keywords

  • surface plasmon resonance
  • insulin-like growth factor (IGF)
  • pharmacological sciences
  • biosensors
  • resonance

Cite this

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abstract = "This review describes a comprehensive analysis of a surface plasmon resonance (SPR)-based biosensor study of molecular interactions in the insulin-like growth factor (IGF) molecular axis. In this study, we focus on the interaction between the polypeptide growth factors IGF-I and IGF-II with six soluble IGF binding proteins (IGFBP 1-6), which occur naturally in various biological fluids. We have describe the conditions required for the accurate determination of kinetic rate constants for these interactions and highlight the experimental and theoretical pitfalls, which may be encountered in the early stages of such a study. We focus on IGFBP-5 and describe a site-directed mutagenesis study, which examines the contribution of various residues in the protein to high affinity interaction with IGF-I and -II. We analyse the interaction of IGFBP-5 (and IGFBP-3) with heparin and other biomolecules and describe experiments, which were designed to monitor multi-protein complex formation in this molecular axis.",
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Molecular interactions in the insulin-like growth factor (IGF) axis: a surface plasmon resonance (SPR) based biosensor study. / Allan, G.J.; Beattie, J.; Shand, J.H.; Szymanowska, M.; Flint, D.J.

In: Molecular and Cellular Biochemistry, Vol. 307, No. 1-2, 2008, p. 221-236.

Research output: Contribution to journalArticle

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T1 - Molecular interactions in the insulin-like growth factor (IGF) axis: a surface plasmon resonance (SPR) based biosensor study

AU - Allan, G.J.

AU - Beattie, J.

AU - Shand, J.H.

AU - Szymanowska, M.

AU - Flint, D.J.

PY - 2008

Y1 - 2008

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AB - This review describes a comprehensive analysis of a surface plasmon resonance (SPR)-based biosensor study of molecular interactions in the insulin-like growth factor (IGF) molecular axis. In this study, we focus on the interaction between the polypeptide growth factors IGF-I and IGF-II with six soluble IGF binding proteins (IGFBP 1-6), which occur naturally in various biological fluids. We have describe the conditions required for the accurate determination of kinetic rate constants for these interactions and highlight the experimental and theoretical pitfalls, which may be encountered in the early stages of such a study. We focus on IGFBP-5 and describe a site-directed mutagenesis study, which examines the contribution of various residues in the protein to high affinity interaction with IGF-I and -II. We analyse the interaction of IGFBP-5 (and IGFBP-3) with heparin and other biomolecules and describe experiments, which were designed to monitor multi-protein complex formation in this molecular axis.

KW - surface plasmon resonance

KW - insulin-like growth factor (IGF)

KW - pharmacological sciences

KW - biosensors

KW - resonance

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