6533b821fe1ef96bd127ba8d

RESEARCH PRODUCT

Fluorescent Small Molecule Probe to Modulate and Explore α2β1 Integrin Function

Olli T. PentikäinenJarkko T. KoivunenLiisa NissinenJuhani HuuskonenJyrki HeinoAnne MarjamäkiJohanna JokinenMarjo PihlavistoJarmo Käpylä

subject

Models MolecularCellIntegrinBiochemistryCatalysisExtracellular matrixColloid and Surface ChemistryCell surface receptormedicineHumansta116Fluorescent DyesBinding SitesbiologyChemistryta1182General ChemistryFluorescenceSmall moleculeSpectrometry Fluorescencemedicine.anatomical_structureBiochemistryBiophysicsbiology.proteinCollagenα2β1 integrinIntegrin alpha2beta1Function (biology)Protein Binding

description

Collagen binding integrins are an important family of cell surface receptors that mediate bidirectionally signals between the interior of the cell and the extracellular matrix. The protein-protein interactions between cells and collagen are necessary for many physiological functions, but also promote diseases. For example, the interaction of α2β1 integrin and collagen has been shown to have an important role in thrombus formation and cancer spread. The fact that the discovery of small molecules that can block such protein-protein interactions is highly challenging has significantly hindered the discovery of pharmaceutical agents to treat these diseases. Here, we present a rationally designed novel fluorescent molecule that can be synthesized in just a few minutes from commercially available starting materials. This molecule blocks the protein-protein interaction between α2β1 integrin and collagen, and due to its fluorescent properties, it can be employed in wide variety of biological applications.

yearjournalcountryeditionlanguage
2011-08-30Journal of the American Chemical Society
https://doi.org/10.1021/ja206086c