Biosensor measurement of the binding of insulin-like growth factors I and II and their analogues to the insulin-like growth factor-binding protein-3.

Heding A, Gill R, Ogawa Y, De Meyts P, Shymko RM

The Journal of biological chemistry1 Jun 1996Cited by 38 (Europe PMC)

PMID8662901DOI10.1074/jbc.271.24.13948PepBankPUB-08662901

Summary

Most insulin-like growth factor (IGF) molecules in the circulation are found in a 150-kDa complex containing IGF-binding protein-3 (IGFBP-3) and an acid-labile subunit, which does not itself bind IGF. Affinities (Kd values) between 0.03 and 0.5 nM have been reported for IGF-I/IGFBP-3 binding, but no kinetic data are available. In this study we measured the high affinity binding of unlabeled IGFs and IGF analogues to recombinant unglycosylated IGFBP-3, using a BIAcoretrade mark instrument (Pharmacia Biosensor AB). IGF-I binding showed fast association and slow non-first-order dissociation kinetics, and an equilibrium Kd of 0.23 nM. IGF-II had similar kinetics with slightly higher affinity. Analogues with mutations in the first 3 amino acids of the B-region (des(1-3) IGF-I and long IGF-I) showed 25 and 50 times lower affinity than IGF-I. Replacement of residues 28-37 by Gly-Gly-Gly-Gly or deletion of residues 29-41 in the C-region had little effect on the kinetic parameters, contrasting with the markedly impaired binding of these analogues to the IGF-I receptor. Swapping of the disulfide bridges in IGF-I and the C-region mutants decreased the affinity dramatically for IGFBP-3, primarily by decreasing the association rate. Insulin had approximately 1000 times lower affinity than IGF-I.

CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study1

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone1

In this study, IGF-1 DES (des(1-3)IGF-I) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking IGF-1 DES (des(1-3)IGF-I).

01LabNot a test of IGF-1 DES (des(1-3)IGF-I) aloneIn vitro (cell-free)Activity measurement
In a biosensor assay, des(1‑3) IGF-I had 25 times lower affinity for IGFBP-3 than IGF-I.
In plain wordsIn lab tests, des(1‑3) IGF-I bound IGFBP-3 with lower affinity than IGF-I.
Peptide
IGF-1 DES (des(1-3)IGF-I)
Outcome
DecreaseIGFBP-3 binding affinity
Study
n: not reported in source
BIAcore binding assay with recombinant unglycosylated IGFBP-3
Comparator
IGF-I
Outcome group
Receptor activity and mechanism · Pharmacology
Measurements
Affinity reduction
25 fold
des(1-3) IGF-I versus IGF-I
Source sentences
Summary
Analogues with mutations in the first 3 amino acids of the B-region (des(1-3) IGF-I and long IGF-I) showed 25 and 50 times lower affinity than IGF-I.
1 context sentence(design, population, supporting numbers)
Summary · context
In this study we measured the high affinity binding of unlabeled IGFs and IGF analogues to recombinant unglycosylated IGFBP-3, using a BIAcoretrade mark instrument (Pharmacia Biosensor AB).
In this study, IGF-1 DES (des(1-3)IGF-I) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking IGF-1 DES (des(1-3)IGF-I).
Show in the study text Report a problemFND-0866290101

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Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

Version 3Current
21 Oct 2026, 15:58 UTC
Study results updated
Version 2
21 Oct 2026, 13:52 UTC
Study data updated · source update from Europe PMC
Version 1
21 Oct 2026, 12:50 UTC
First added · source update from Europe PMC

Subjects

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Publication types

Journal Article

MeSH terms

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