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Extracellular matrix heparin-binding domains

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Jeffrey Alan Hubbell, Mikaël Martino, Federico Tortelli, Jeffrey James Rice
2015

Abstract

Heparin binding peptides derived from a Tenascin (TNC) III1-5 domain or a fibrinogen ²15-66 domain have been found that bind certain cytokines with high affinity. Materials and methods for making compositions and devices using these peptides are disclosed.

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https://infoscience.epfl.ch/entities/publication/b648b8c5-29ab-45de-825c-4b5a0d5276b5

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Related concepts (7)

Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major components of the basal lamina (one of the layers of the basement membrane), the protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion. Laminins are heterotrimeric proteins with a high molecular mass (~400 to ~900 kDa).

Fibronectin is a high-molecular weight (~500-~600 kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. It is approved for marketing as a topical solution in India by Central Drugs Standard Control organization in 2020 under the brand name FIBREGA for chronic wounds. Fibronectin also binds to other extracellular matrix proteins such as collagen, fibrin, and heparan sulfate proteoglycans (e.g. syndecans).

In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions.

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