{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vincenzi M"],"funding":["AIRC","Italian Association for Cancer Research"],"pagination":["10616"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11476629"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(19)"],"pubmed_abstract":["The Sam (Sterile alpha motif) domain of the lipid phosphatase Ship2 (Ship2-Sam) is engaged by the Sam domain of the receptor tyrosine kinase EphA2 (EphA2-Sam) and, this interaction is principally linked to procancer effects. Peptides able to hinder the formation of the EphA2-Sam/Ship2-Sam complex could possess therapeutic potential. Herein, by employing the FoldX software suite, we set up an in silico approach to improve the peptide targeting of the so-called Mid Loop interface of Ship2-Sam, representing the EphA2-Sam binding site. Starting from a formerly identified peptide antagonist of the EphA2-Sam/Ship2-Sam association, first, the most stabilizing mutations that could be inserted in each peptide position were predicted. Then, they were combined, producing a list of potentially enhance"],"journal":["International journal of molecular sciences"],"pubmed_title":["Exploring a Potential Optimization Route for Peptide Ligands of the Sam Domain from the Lipid Phosphatase Ship2."],"pmcid":["PMC11476629"],"funding_grant_id":["26121","IG26121"],"pubmed_authors":["Mercurio FA","Vincenzi M","Marasco D","Palumbo R","Leone M","La Manna S","Pirone L","Pedone EM"],"additional_accession":[]},"is_claimable":false,"name":"Exploring a Potential Optimization Route for Peptide Ligands of the Sam Domain from the Lipid Phosphatase Ship2.","description":"The Sam (Sterile alpha motif) domain of the lipid phosphatase Ship2 (Ship2-Sam) is engaged by the Sam domain of the receptor tyrosine kinase EphA2 (EphA2-Sam) and, this interaction is principally linked to procancer effects. Peptides able to hinder the formation of the EphA2-Sam/Ship2-Sam complex could possess therapeutic potential. Herein, by employing the FoldX software suite, we set up an in silico approach to improve the peptide targeting of the so-called Mid Loop interface of Ship2-Sam, representing the EphA2-Sam binding site. Starting from a formerly identified peptide antagonist of the EphA2-Sam/Ship2-Sam association, first, the most stabilizing mutations that could be inserted in each peptide position were predicted. Then, they were combined, producing a list of potentially enhance","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-06-30T03:17:01.388Z","creation":"2025-04-04T11:05:23.227Z"},"accession":"S-EPMC11476629","cross_references":{"pubmed":["39408946"],"doi":["10.3390/ijms251910616"]}}