Scientific Reports· 2017Q1
A Comprehensive Evaluation of the Activity and Selectivity Profile of Ligands for RGD-binding Integrins
- 614citations
- Q1SCImago
- 2017year
Short summary
This study systematically compares the binding affinity of various ligands for RGD-binding integrins (αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3) using a solid-phase binding assay.
AI-generated from the title and abstract; the full text is not read.
Key points
- Integrins are cell surface receptors critical for cell structure and behavior, implicated in various diseases.
- Many integrin-specific ligands exist, but their reported activity metrics (IC50 values) are inconsistent.
- This study evaluated a broad range of ligands for their binding affinity to RGD-binding integrins.
- A homogenous ELISA-like solid-phase binding assay was used for standardized comparison.
AI-generated from the title and abstract; the full text is not read.
Abstract
Abstract Integrins, a diverse class of heterodimeric cell surface receptors, are key regulators of cell structure and behaviour, affecting cell morphology, proliferation, survival and differentiation. Consequently, mutations in specific integrins, or their deregulated expression, are associated with a variety of diseases. In the last decades, many integrin-specific ligands have been developed and used for modulation of integrin function in medical as well as biophysical studies. The IC 50 -values reported for these ligands strongly vary and are measured using different cell-based and cell-free systems. A systematic comparison of these values is of high importance for selecting the optimal ligands for given applications. In this study, we evaluate a wide range of ligands for their binding affinity towards the RGD-binding integrins αvβ3, αvβ5, αvβ6, αvβ8, α5β1, αIIbβ3, using homogenous ELISA-like solid phase binding assay.
The authors' abstract, as published at the source. Scientific Reports, 2017 · DOI ↗
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Field: Immunology and Allergy
Immunology and AllergyMedicine