{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dang VT"],"funding":["Michigan Technology Tri-Corridor","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["2304-2308"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12857771"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(7)"],"pubmed_abstract":["β-Barrels are ubiquitous motifs in protein structures, but the fundamental rules underlying their formation are unclear, and their <i>de novo</i> design remains highly challenging. Small peptides that form barrels are especially scarce. Here, we report barrels with the shortest staves (6 residues, ∼60% of previous record) and smallest shear number (<i>S</i> = 4) so far, formed from 12-residue macrocyclic peptides. The miniature barrel has anomalous structural features, demonstrated by solution phase and crystallographic characterization; there is a pronounced and essential backbone kink imparted by an achiral residue, <i>N</i>-methylglycine, as well as four structural water molecules stitching the seams of the barrel. These results provide insights into how extremely short sequences could form barrel assemblies."],"journal":["Chemical communications (Cambridge, England)"],"pubmed_title":["β-barrels from short macrocyclic peptides."],"pmcid":["PMC12857771"],"funding_grant_id":["R35GM154793","085P1000817","R35 GM154793"],"pubmed_authors":["McElheny D","Dang VT","Nguyen AI","Martynowycz MW"],"additional_accession":[]},"is_claimable":false,"name":"β-barrels from short macrocyclic peptides.","description":"β-Barrels are ubiquitous motifs in protein structures, but the fundamental rules underlying their formation are unclear, and their <i>de novo</i> design remains highly challenging. Small peptides that form barrels are especially scarce. Here, we report barrels with the shortest staves (6 residues, ∼60% of previous record) and smallest shear number (<i>S</i> = 4) so far, formed from 12-residue macrocyclic peptides. The miniature barrel has anomalous structural features, demonstrated by solution phase and crystallographic characterization; there is a pronounced and essential backbone kink imparted by an achiral residue, <i>N</i>-methylglycine, as well as four structural water molecules stitching the seams of the barrel. These results provide insights into how extremely short sequences could form barrel assemblies.","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-16T07:26:39.788Z","creation":"2026-06-16T03:10:09.175Z"},"accession":"S-EPMC12857771","cross_references":{"pubmed":["41489626"],"doi":["10.1039/d5cc06640a"]}}