Assessing a computational pipeline to identify binding motifs to the α2β1 integrin

Integrins in the cell surface interact with functional motifs found in the extracellular matrix (ECM) that queue the cell for biological actions such as migration, adhesion, or growth. Multiple fibrous proteins such as collagen or fibronectin compose the ECM. The field of biomechanical engineering often deals with the design of biomaterials compatible with the ECM that will trigger cellular response (e.g., in tissue regeneration). However, there are a relative few number of known integrin binding motifs compared to all the possible peptide epitope sequences available. Computational tools could help identify novel motifs, but have been limited by the challenges in modeling the binding to integrin domains. We revisit a series of traditional and novel computational tools to assess their performance in identifying novel binding motifs for the I-domain of the α2β1 integrin.

Abstract licence: CC BY

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