{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ding L"],"funding":["National Natural Science Foundation of China","the Natural Science Foundation of Hubei Province"],"pagination":["23"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11769409"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["Coagulation factor XIa is a new serine-protease family drug target for next-generation anticoagulants. With the snake venom Kunitz-type peptide BF9 as the scaffold, we obtained a highly active XIa inhibitor BF9-N17K in our previous work, but it also inhibited the hemostatic target plasmin. Here, in order to enhance the selectivity of BF9-N17K toward XIa, four mutants, BF9-N17K-L19A, BF9-N17K-L19S, BF9-N17K-L19D, and BF9-N17K-L19K, were further designed using the P2' amino acid classification scanning strategy. The anticoagulation assay showed that the four P2' single-point mutants still had apparent inhibitory anticoagulation activity that selectively inhibited the human intrinsic coagulation pathway and had no influence on the extrinsic coagulation pathway or common coagulation pathway, w"],"journal":["Toxins"],"pubmed_title":["Improvement in XIa Selectivity of Snake Venom Peptide Analogue BF9-N17K Using P2' Amino Acid Replacements."],"pmcid":["PMC11769409"],"funding_grant_id":["81973321 and 82204407","2021CFB130"],"pubmed_authors":["Chen Z","Lin Y","Sun F","Zhai Z","Luo H","Zhu W","Luo X","Qin T","Ye X","Ding L","Shuang Z","Qin C"],"additional_accession":[]},"is_claimable":false,"name":"Improvement in XIa Selectivity of Snake Venom Peptide Analogue BF9-N17K Using P2' Amino Acid Replacements.","description":"Coagulation factor XIa is a new serine-protease family drug target for next-generation anticoagulants. With the snake venom Kunitz-type peptide BF9 as the scaffold, we obtained a highly active XIa inhibitor BF9-N17K in our previous work, but it also inhibited the hemostatic target plasmin. Here, in order to enhance the selectivity of BF9-N17K toward XIa, four mutants, BF9-N17K-L19A, BF9-N17K-L19S, BF9-N17K-L19D, and BF9-N17K-L19K, were further designed using the P2' amino acid classification scanning strategy. The anticoagulation assay showed that the four P2' single-point mutants still had apparent inhibitory anticoagulation activity that selectively inhibited the human intrinsic coagulation pathway and had no influence on the extrinsic coagulation pathway or common coagulation pathway, w","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2025-04-05T09:33:26.418Z","creation":"2025-04-05T09:33:26.418Z"},"accession":"S-EPMC11769409","cross_references":{"pubmed":["39852976"],"doi":["10.3390/toxins17010023"]}}