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Targeting ADAM proteases, particularly ADAM10, holds promise for fine\u2010tuning inflammatory responses. However, developing selective inhibitors has proven challenging because of cross\u2010inhibition of other metalloproteases. Protein\u2010based inhibitors, such as the synthetic ADAM10 prodomain, offer potential for improved selectivity and effectiveness.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Experimental Approach<\/jats:title>\n                    <jats:p>A novel ADAM10 inhibitor, VTH144, was designed by modifying the ADAM10 prodomain and evaluated empirically for selectivity, efficacy and toxicity both in vitro and in vivo and by using machine learning\u2013based modelling.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Key Results<\/jats:title>\n                    <jats:p>\n                      AlphaFold3 predictions confirm that the ADAM10 prodomain is highly selective for its protease and identify VTH144 as a unique ADAM10\u2010inhibiting peptide. Fluorescence resonance energy transfer (FRET) assays verified VTH144 as highly selective for ADAM10, sparing other metalloproteases. In a MI mouse model, we show that VTH144 applied twice, 4 and 48\u2009h after ligation of the left ventricular descending artery (LAD), is highly effective in preserving cardiac function by reducing scar size. VTH144 significantly attenuates ADAM10\u2010mediated CX\n                      <jats:sub>3<\/jats:sub>\n                      CL1 shedding, subsequent neutrophil infiltration into the heart and IL\u20101\u03b2\u2010driven systemic inflammation. Importantly, safety pharmacology in na\u00efve mice revealed that ADAM10 inhibition with VTH144 lacks toxic short\u2010term effects in cardiac, pulmonary, hepatic or renal systems.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions and Implications<\/jats:title>\n                    <jats:p>Our study highlights the potential of the selective ADAM10 inhibitor VTH144 as a promising therapeutic candidate for improving cardiac function and reducing the risk of heart failure following myocardial infarction.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/bph.70201","type":"journal-article","created":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T06:20:46Z","timestamp":1759990846000},"page":"990-1008","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Leveraging the ADAM10 prodomain for selective inhibition to enhance 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