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Study · In vitro (cell-free) · 2001

3 results

BIAcore analysis of bovine insulin-like growth factor (IGF)-binding protein-2 identifies major IGF binding site determinants in both the amino- and carboxyl-terminal domains.

Carrick FE, Forbes BE, Wallace JC

The Journal of biological chemistry16 May 2001Cited by 41 (Europe PMC)

PMID11356837 (opens in a new tab)DOI10.1074/jbc.m101317200 (opens in a new tab)PepBankPUB-11356837
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Summary

In the absence of a complete tertiary structure to define the molecular basis of the high affinity binding interaction between insulin-like growth factors (IGFs) and IGF-binding proteins (IGFBPs), we have investigated binding of IGFs by discrete amino-terminal domains (amino acid residues 1-93, 1-104, 1-132, and 1-185) and carboxyl-terminal domains (amino acid residues 96-279, 136-279, and 182-284) of bovine IGFBP-2 (bIGFBP-2). Both halves of bIGFBP-2 bound IGF-I and IGF-II in BIAcore studies, albeit with different affinities ((1-132)IGFBP-2, K(D) = 36.3 and 51.8 nm; (136-279)IGFBP-2HIS, K(D) = 23.8 and 16.3 nm, respectively). The amino-terminal half appears to contain components responsible for fast association. In contrast, IGF binding by the carboxyl-terminal fragment results in a more stable complex as reflected by its K(D). Furthermore, des(1-3)IGF-I and des(1-6)IGF-II exhibited reduced binding affinity to (1-279)IGFBP-2HIS, (1-132)IGFBP-2, and (136-279)IGFBP-2HIS biosensor surfaces compared with wild-type IGF. A charge reversal at positions 3 and 6 of IGF-I and IGF-II, respectively, affects binding interactions with the amino-terminal fragment and full-length bIGFBP-2 but not the carboxyl-terminal fragment.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study3

3 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Activity measurement

    In BIAcore assays, des(1‑3)IGF-I had lower affinity for (1-279)IGFBP-2HIS than wild-type IGF.

    In plain wordsIn lab tests, des(1‑3)IGF-I bound full-length IGFBP-2 less strongly than wild-type IGF.

    Peptide
    IGF-1 DES (des(1-3)IGF-I)
    Outcome
    DecreaseBinding affinity to full-length IGFBP-2
    Study

    n: not reported in source

    BIAcore biosensor surfaces
    Comparator
    Wild-type IGF
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Furthermore, des(1-3)IGF-I and des(1-6)IGF-II exhibited reduced binding affinity to (1-279)IGFBP-2HIS, (1-132)IGFBP-2, and (136-279)IGFBP-2HIS biosensor surfaces compared with wild-type IGF.
  2. 02LabIn vitro (cell-free)Activity measurement

    In BIAcore assays, des(1‑3)IGF-I had lower affinity for (1-132)IGFBP-2 than wild-type IGF.

    In plain wordsIn lab tests, des(1‑3)IGF-I bound the amino-terminal IGFBP-2 fragment less strongly than wild-type IGF.

    Peptide
    IGF-1 DES (des(1-3)IGF-I)
    Outcome
    DecreaseBinding affinity to amino-terminal IGFBP-2
    Study

    n: not reported in source

    BIAcore biosensor surfaces
    Comparator
    Wild-type IGF
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Furthermore, des(1-3)IGF-I and des(1-6)IGF-II exhibited reduced binding affinity to (1-279)IGFBP-2HIS, (1-132)IGFBP-2, and (136-279)IGFBP-2HIS biosensor surfaces compared with wild-type IGF.
  3. 03LabIn vitro (cell-free)Activity measurement

    In BIAcore assays, des(1‑3)IGF-I had lower affinity for (136-279)IGFBP-2HIS than wild-type IGF.

    In plain wordsIn lab tests, des(1‑3)IGF-I bound the carboxyl-terminal IGFBP-2 fragment less strongly than wild-type IGF.

    Peptide
    IGF-1 DES (des(1-3)IGF-I)
    Outcome
    DecreaseBinding affinity to carboxyl-terminal IGFBP-2
    Study

    n: not reported in source

    BIAcore biosensor surfaces
    Comparator
    Wild-type IGF
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Furthermore, des(1-3)IGF-I and des(1-6)IGF-II exhibited reduced binding affinity to (1-279)IGFBP-2HIS, (1-132)IGFBP-2, and (136-279)IGFBP-2HIS biosensor surfaces compared with wild-type IGF.

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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.

  1. Version 3Current

    21 Oct 2026, 15:58 UTC

    Study results updated

  2. Version 2

    21 Oct 2026, 13:52 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    21 Oct 2026, 12:50 UTC

    First added · source update from Europe PMC

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