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The development of peptide inhibitors is a promising approach to modulate the interaction of Sema\u20103A with its receptor NRP\u20101. Few interaction points between these binding partners are known. However, an immunoglobulin\u2010like domain\u2010derived peptide of Sema\u20103A has shown a positive effect on cell proliferation. To specify these interactions between the peptide inhibitor and the Sema\u20103A\u2013NRP\u20101 system, the peptides were modified with the photoactivatable amino acids 4\u2010benzoyl\u2010<jats:sc>l<\/jats:sc>\u2010phenylalanine or photo\u2010<jats:sc>l<\/jats:sc>\u2010leucine by solid\u2010phase peptide synthesis. Activity was tested by an enzyme\u2010linked immunosorbent\u2010based binding assay, and crosslinking experiments were analyzed by Western blot and mass spectrometry, demonstrating a specific binding site of the peptide at Sema\u20103A. The observed signals for Sema\u20103A\u2010peptide interaction were found in a defined area of the Sema domain, which was also demonstrated to be involved in NRP\u20101 binding. The presented data identified the interaction site for further development of therapeutic peptides to treat acute kidney injury by blocking the Sema\u20103A\u2013NRP\u20101 interaction.<\/jats:p>","DOI":"10.1002\/psc.3460","type":"journal-article","created":{"date-parts":[[2022,10,26]],"date-time":"2022-10-26T11:12:54Z","timestamp":1666782774000},"update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Pinpointing the interaction site between semaphorin\u20103A and its inhibitory peptide"],"prefix":"10.1002","volume":"29","author":[{"given":"Kevin","family":"Kretschmer","sequence":"first","affiliation":[{"name":"Institute of Biochemistry, Faculty of Life Sciences Leipzig University Leipzig Germany"}]},{"given":"Jan","family":"Stichel","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Faculty of Life Sciences Leipzig University Leipzig 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