{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gray VP"],"funding":["Division of Materials Research"],"pagination":["5273-5280"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11323006"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(8)"],"pubmed_abstract":["Coiled coils, commonly found in native proteins, are helical motifs important for mediating intermolecular interactions. While coiled coils are attractive for use in new therapies and biomaterials, the lack of enzymatic stability of naturally occurring l-peptides may limit their implementation in biological environments. d-peptides are of interest for biomedical applications as they are resistant to enzymatic degradation and recent reports indicate that stereochemistry-driven interactions, achieved by blending d- and l-peptides, yield access to a greater range of binding affinities and a resistance to enzymatic degradation compared to l-peptides alone. To our knowledge, this effect has not been studied in coiled coils. Here, we investigate the effects of blending heterochiral E/K coiled co"],"journal":["Biomacromolecules"],"pubmed_title":["Designing Coiled Coils for Heterochiral Complexation to Enhance Binding and Enzymatic Stability."],"pmcid":["PMC11323006"],"funding_grant_id":["BMAT-2143647"],"pubmed_authors":["Letteri RA","Gray VP"],"additional_accession":[]},"is_claimable":false,"name":"Designing Coiled Coils for Heterochiral Complexation to Enhance Binding and Enzymatic Stability.","description":"Coiled coils, commonly found in native proteins, are helical motifs important for mediating intermolecular interactions. While coiled coils are attractive for use in new therapies and biomaterials, the lack of enzymatic stability of naturally occurring l-peptides may limit their implementation in biological environments. d-peptides are of interest for biomedical applications as they are resistant to enzymatic degradation and recent reports indicate that stereochemistry-driven interactions, achieved by blending d- and l-peptides, yield access to a greater range of binding affinities and a resistance to enzymatic degradation compared to l-peptides alone. To our knowledge, this effect has not been studied in coiled coils. Here, we investigate the effects of blending heterochiral E/K coiled co","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Aug","modification":"2025-04-26T21:21:41.395Z","creation":"2025-04-06T16:44:59.593Z"},"accession":"S-EPMC11323006","cross_references":{"pubmed":["38980285"],"doi":["10.1021/acs.biomac.4c00661"]}}