{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13(26)"],"submitter":["Li X"],"funding":["National Institutes of Health"],"pubmed_abstract":["In 1953, Pauling and Corey postulated \"rippled\" β-sheets, composed of a mixture of d- and l-peptide strands, as a hypothetical alternative to the now well-established structures of \"pleated\" β-sheets, which they proposed as a component of all-l-proteins. Growing interest in rippled β-sheets over the past decade has led to the development of mixtures of d- and l-peptides for biomedical applications, and a theory has emerged that mixtures of enantiomeric β-sheet peptides prefer to co-assemble in a heterochiral fashion to form rippled β-sheets. Intrigued by conflicting reports that enantiomeric β-sheet peptides prefer to self-assemble in a homochiral fashion to form pleated β-sheets, we set out address this controversy using two β-sheet peptides derived from Aβ<sub>17-23</sub> and Aβ<sub>30-36</sub>, peptides 1a and 1b. Each of these peptides self-assembles to form tetramers comprising sandwiches of β-sheet dimers in aqueous solution. Through solution-phase NMR spectroscopy, we characterize the different species formed when peptides 1a and 1b are mixed with their respective d-enantiomers, peptides <i>ent</i>-1a and <i>ent</i>-1b. <sup>1</sup>H NMR, DOSY, and <sup>1</sup>H,<sup>15</sup>N-HSQC experiments reveal that mixing peptides 1a and <i>ent</i>-1a results in the predominant formation of homochiral tetramers, with a smaller fraction of a new heterochiral tetramer, and mixing peptides 1b and <i>ent</i>-1b does not result in any detectable heterochiral assembly. <sup>15</sup>N-edited NOESY reveals that the heterochiral tetramer formed by peptides 1a and <i>ent</i>-1a is composed of two homochiral dimers. Collectively, these NMR studies of Aβ-derived peptides provide compelling evidence that enantiomeric β-sheet peptides prefer to self-assemble in a homochiral fashion in aqueous solution."],"journal":["Chemical science"],"pagination":["7739-7746"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9258340"],"repository":["biostudies-literature"],"pubmed_title":["Enantiomeric β-sheet peptides from Aβ form homochiral pleated β-sheets rather than heterochiral rippled β-sheets."],"pmcid":["PMC9258340"],"pubmed_authors":["Li X","Rios SE","Nowick JS"],"additional_accession":[]},"is_claimable":false,"name":"Enantiomeric β-sheet peptides from Aβ form homochiral pleated β-sheets rather than heterochiral rippled β-sheets.","description":"In 1953, Pauling and Corey postulated \"rippled\" β-sheets, composed of a mixture of d- and l-peptide strands, as a hypothetical alternative to the now well-established structures of \"pleated\" β-sheets, which they proposed as a component of all-l-proteins. Growing interest in rippled β-sheets over the past decade has led to the development of mixtures of d- and l-peptides for biomedical applications, and a theory has emerged that mixtures of enantiomeric β-sheet peptides prefer to co-assemble in a heterochiral fashion to form rippled β-sheets. Intrigued by conflicting reports that enantiomeric β-sheet peptides prefer to self-assemble in a homochiral fashion to form pleated β-sheets, we set out address this controversy using two β-sheet peptides derived from Aβ<sub>17-23</sub> and Aβ<sub>30-36</sub>, peptides 1a and 1b. Each of these peptides self-assembles to form tetramers comprising sandwiches of β-sheet dimers in aqueous solution. Through solution-phase NMR spectroscopy, we characterize the different species formed when peptides 1a and 1b are mixed with their respective d-enantiomers, peptides <i>ent</i>-1a and <i>ent</i>-1b. <sup>1</sup>H NMR, DOSY, and <sup>1</sup>H,<sup>15</sup>N-HSQC experiments reveal that mixing peptides 1a and <i>ent</i>-1a results in the predominant formation of homochiral tetramers, with a smaller fraction of a new heterochiral tetramer, and mixing peptides 1b and <i>ent</i>-1b does not result in any detectable heterochiral assembly. <sup>15</sup>N-edited NOESY reveals that the heterochiral tetramer formed by peptides 1a and <i>ent</i>-1a is composed of two homochiral dimers. Collectively, these NMR studies of Aβ-derived peptides provide compelling evidence that enantiomeric β-sheet peptides prefer to self-assemble in a homochiral fashion in aqueous solution.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2025-04-05T14:26:09.741Z","creation":"2025-04-05T14:26:09.741Z"},"accession":"S-EPMC9258340","cross_references":{"pubmed":["35865901"],"doi":["10.1039/d2sc02080g"]}}