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.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Beattie J,Phillips K,Shand JH,Szymanowska M,Flint DJ,Allan GJdoi
10.1007/s11010-007-9601-8subject
Has Abstractpub_date
2008-01-01 00:00:00pages
221-36issue
1-2eissn
0300-8177issn
1573-4919journal_volume
307pub_type
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journal_title:Molecular and cellular biochemistry
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