{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rodriguez-Alfonso A"],"funding":["Deutsche Forschungsgemeinschaft","Ulm University","German Research Foundation (DFG)","Baden-Württemberg Stiftung","University of Ulm"],"pagination":["15029"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9735595"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(23)"],"pubmed_abstract":["Advanced derivatives of the <b>E</b>ndogenous <b>P</b>eptide <b>I</b>nhibitor of C<b>X</b>CR<b>4</b> (EPI-X4) have shown therapeutic efficacy upon topical administration in animal models of asthma and dermatitis. Here, we studied the plasma stability of the EPI-X4 lead compounds WSC02 and JM#21, using mass spectrometry to monitor the chemical integrity of the peptides and a functional fluorescence-based assay to determine peptide function in a CXCR4-antibody competition assay. Although mass spectrometry revealed very rapid disappearance of both peptides in human plasma within seconds, the functional assay revealed a significantly higher half-life of 9 min for EPI-X4 WSC02 and 6 min for EPI-X4 JM#21. Further analyses demonstrated that EPI-X4 WSC02 and EPI-X4 JM#21 interact with low molecula"],"journal":["International journal of molecular sciences"],"pubmed_title":["Advanced EPI-X4 Derivatives Covalently Bind Human Serum Albumin Resulting in Prolonged Plasma Stability."],"pmcid":["PMC9735595"],"funding_grant_id":["EXC 2033 - 390677874 614 - RESOLV","CRC1279","MU 3115/8-1","L.SBN.0209","3115/11-1","436586093","EXC 2033—390677874—RESOLV","BWST_WSF-025"],"pubmed_authors":["Kuan SL","Weil T","Munch J","Ruiz-Blanco YB","Standker L","Wiese S","Sanchez-Garcia E","Heck A","Gilg A","Harms M","Rodriguez-Alfonso A"],"additional_accession":[]},"is_claimable":false,"name":"Advanced EPI-X4 Derivatives Covalently Bind Human Serum Albumin Resulting in Prolonged Plasma Stability.","description":"Advanced derivatives of the <b>E</b>ndogenous <b>P</b>eptide <b>I</b>nhibitor of C<b>X</b>CR<b>4</b> (EPI-X4) have shown therapeutic efficacy upon topical administration in animal models of asthma and dermatitis. Here, we studied the plasma stability of the EPI-X4 lead compounds WSC02 and JM#21, using mass spectrometry to monitor the chemical integrity of the peptides and a functional fluorescence-based assay to determine peptide function in a CXCR4-antibody competition assay. Although mass spectrometry revealed very rapid disappearance of both peptides in human plasma within seconds, the functional assay revealed a significantly higher half-life of 9 min for EPI-X4 WSC02 and 6 min for EPI-X4 JM#21. Further analyses demonstrated that EPI-X4 WSC02 and EPI-X4 JM#21 interact with low molecula","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-04-08T11:58:34.924Z","creation":"2025-04-19T12:16:18.078Z"},"accession":"S-EPMC9735595","cross_references":{"pubmed":["36499357"],"doi":["10.3390/ijms232315029"]}}