Myo-inositol hexasulphate and low molecular weight heparin binding to human acidic fibroblast growth factor: a calorimetric and FTIR study.

@article{GuzmnCasado2001MyoinositolHA,
  title={Myo-inositol hexasulphate and low molecular weight heparin binding to human acidic fibroblast growth factor: a calorimetric and FTIR study.},
  author={Mercedes Guzm{\'a}n-Casado and Antonio Cardenete and Guillermo Gim{\'e}nez-Gallego and Antonio Parody-Morreale},
  journal={International journal of biological macromolecules},
  year={2001},
  volume={28 4},
  pages={
          305-13
        },
  url={https://api.semanticscholar.org/CorpusID:21387118}
}
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42 References

Effect of polyanions on the refolding of human acidic fibroblast growth factor.

1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate.

The computed three-dimensional structure suggests that inositol hexasulfate may stabilize and activate the protein by conferring rigidity to the hairpin involving beta-strands 10 and 11.

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Heparin Structure and Interactions with Basic Fibroblast Growth Factor

No significant conformational change in bFGF occurred upon heparin oligosaccharide binding, which suggests that heparIn primarily serves to juxtapose components of the FGF signal transduction pathway.

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The combination of site-directed mutagenesis and titrating calorimetry permitted an analysis of the energetic contributions of individual bF GF residues in the binding of heparin to bFGF, indicating that pure electrostatic interactions contribute only 30% of the binding free energy as analyzed by polyelectrolyte theory and that more specific nonionic interactions, such as hydrogen bonding and van der Waals packing, contribute the majority of the free energy for this binding reaction.

Nature of the interaction of heparin with acidic fibroblast growth factor.

AFGF appears to bind at high density (one molecule every 4-5 polysaccharide units) and with high affinity to heparin, which potentially provides a concentrated, stabilized storage form of the growth factor that can be released for receptor-mediated cellular activation in response to the proper stimuli.

Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog.

The data suggest that enhancement of structural definition may play a key role in the modulation of the affinity of aFGF by its receptor, and, consequently, of its specific mitogenic activity.

Binding of heparin to basic fibroblast growth factor induces a conformational change.

Physical stabilization of acidic fibroblast growth factor by polyanions.

A wide variety of well-defined polyanions are investigated in terms of their ability to stabilize human recombinant aFGF against thermal denaturation based on the X-ray crystal structure of the bovine protein and previous studies of the heparin binding site of both acidic and basic FGF.

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