{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T22:47:17Z","timestamp":1790808437673,"version":"4.1.0"},"reference-count":31,"publisher":"S. Karger AG","issue":"3-4","license":[{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"},{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.karger.com\/Services\/SiteLicenses"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmacology"],"published-print":{"date-parts":[[2016]]},"abstract":"<jats:p>A20FMDV2 is a peptide derived from the foot-and-mouth disease virus with a high affinity and selectivity for the alpha-v beta-6 (\u03b1v\u03b26) arginyl-glycinyl-aspartic acid (RGD)-binding integrin. It has been shown to be an informative tool ligand in pre-clinical imaging studies for selective labelling of the \u03b1v\u03b26 integrin in a number of disease models. In a radioligand binding assay using a radiolabelled form of the peptide ([&lt;sup&gt;3&lt;\/sup&gt;H]A20FMDV2), its high affinity (K&lt;sub&gt;D&lt;\/sub&gt;: 0.22 nmol\/l) and selectivity (at least 85-fold) for \u03b1v\u03b26 over the other members of the RGD integrin family was confirmed. [&lt;sup&gt;3&lt;\/sup&gt;H]A20FMDV2 \u03b1v\u03b26 binding could be fully reversed only in the presence of EDTA, whereas a partial reversal was observed in the presence of excess concentrations of an RGD-mimetic small molecule (SC-68448) or unlabelled A20FMDV2. Using flow cytometry on bronchial epithelial cells, the ligand-induced internalization of \u03b1v\u03b26 by A20FMDV2 and latency-associated peptide-1 was shown to be fast (t&lt;sub&gt;1\/2&lt;\/sub&gt;: 1.5 and 3.1 min, respectively), concentration-dependent (EC&lt;sub&gt;50&lt;\/sub&gt;: values 1.1 and 3.6 nmol\/l, respectively) and was followed by a moderately slow return of integrin to the surface. The results of the radioligand binding studies suggest that the binding of A20FMDV2 to the RGD-binding site on \u03b1v\u03b26 is required to maintain its engagement with the hypothesised A20FMDV2 synergy site on the integrin. In addition, there is evidence from flow cytometric studies that the RGD-ligand engagement of \u03b1v\u03b26 post-internalization plays a role in delaying recycling of the integrin to the cell surface. This mechanism may act as a homeostatic control of membrane \u03b1v\u03b26 following RGD ligand engagement.<\/jats:p>","DOI":"10.1159\/000443180","type":"journal-article","created":{"date-parts":[[2016,1,6]],"date-time":"2016-01-06T22:01:24Z","timestamp":1452117684000},"page":"114-125","source":"Crossref","is-referenced-by-count":31,"title":["Pharmacological Characterization of the \u03b1v\u03b26 Integrin Binding and Internalization Kinetics of the Foot-and-Mouth Disease Virus Derived Peptide A20FMDV2"],"prefix":"10.1159","volume":"97","author":[{"given":"Robert J.","family":"Slack","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maryam","family":"Hafeji","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca","family":"Rogers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steve 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