{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bera S"],"funding":["European Research Council"],"pagination":["503-509"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7616940"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(5)"],"pubmed_abstract":["The structural versatility, biocompatibility and dynamic range of the mechanical properties of protein materials have been explored in functional biomaterials for a wide array of biotechnology applications. Typically, such materials are made from self-assembled peptides with a predominant β-sheet structure, a common structural motif in silk and amyloid fibrils. However, collagen, the most abundant protein in mammals, is based on a helical arrangement. Here we show that Pro-Phe-Phe, the most aggregation-prone tripeptide of natural amino acids, assembles into a helical-like sheet that is stabilized by the dry hydrophobic interfaces of Phe residues. This architecture resembles that of the functional PSMα3 amyloid, highlighting the role of dry helical interfaces as a core structural motif in amyloids. Proline replacement by hydroxyproline, a major constituent of collagen, generates minimal helical-like assemblies with enhanced mechanical rigidity. These results establish a framework for designing functional biomaterials based on ultrashort helical protein elements."],"journal":["Nature materials"],"pubmed_title":["Rigid helical-like assemblies from a self-aggregating tripeptide."],"pmcid":["PMC7616940"],"funding_grant_id":["694426"],"pubmed_authors":["Bera S","Mondal S","Xue B","Shimon LJW","Cao Y","Gazit E"],"additional_accession":[]},"is_claimable":false,"name":"Rigid helical-like assemblies from a self-aggregating tripeptide.","description":"The structural versatility, biocompatibility and dynamic range of the mechanical properties of protein materials have been explored in functional biomaterials for a wide array of biotechnology applications. Typically, such materials are made from self-assembled peptides with a predominant β-sheet structure, a common structural motif in silk and amyloid fibrils. However, collagen, the most abundant protein in mammals, is based on a helical arrangement. Here we show that Pro-Phe-Phe, the most aggregation-prone tripeptide of natural amino acids, assembles into a helical-like sheet that is stabilized by the dry hydrophobic interfaces of Phe residues. This architecture resembles that of the functional PSMα3 amyloid, highlighting the role of dry helical interfaces as a core structural motif in amyloids. Proline replacement by hydroxyproline, a major constituent of collagen, generates minimal helical-like assemblies with enhanced mechanical rigidity. These results establish a framework for designing functional biomaterials based on ultrashort helical protein elements.","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May","modification":"2026-04-08T19:49:11.841Z","creation":"2025-04-04T12:25:33.765Z"},"accession":"S-EPMC7616940","cross_references":{"pubmed":["30988450"],"doi":["10.1038/s41563-019-0343-2"]}}