biostudies-literatureLiu XNSFNCRR NIH HHSU.S. Department of AgricultureUniversity of Wisconsin-MadisonNational Institutes of HealthUSDANIGMS NIH HHSNIH HHSNational Science Foundation2772-2776https://www.ebi.ac.uk/biostudies/studies/S-EPMC8486351biostudies-literatureUnknown22(18)Assemblies of racemic β-sheet-forming peptides have attracted attention for biomedical applications because racemic forms of peptides can self-associate more avidly than do single enantiomers. In 1953, Pauling and Corey proposed "rippled β-sheet" modes of H-bond-mediated interstrand assembly for alternating L- and D-peptide strands; this structural hypothesis was complementary to their proposal of "pleated β-sheet" assembly for L-peptides. Although no high-resolution structure has been reported for a rippled β-sheet, there is strong evidence for the occurrence of rippled β-sheets in some racemic peptide assemblies. Here we compare propensities of peptide diastereomers in aqueous solution to form a minimum increment of β-sheet in which two antiparallel strands associate. β-Hairpin folding iChembiochem : a European journal of chemical biologyComparisons of β-Hairpin Propensity Among Peptides with Homochiral or Heterochiral Strands.PMC8486351S10RR025062S10 RR023438P41GM136463S10RR029220S10 OD012245OIA-9977486P41 RR002301R01GM061238R01 GM061238P41RR002301S10 RR029220S10RR023438S10RR08438DMB-8415048S10 RR025062S10RR02781S10 RR008438BIR-9214394P41 GM103399S10 RR002781P41 GM136463P41GM103399Liu XGellman SHfalseComparisons of β-Hairpin Propensity Among Peptides with Homochiral or Heterochiral Strands.Assemblies of racemic β-sheet-forming peptides have attracted attention for biomedical applications because racemic forms of peptides can self-associate more avidly than do single enantiomers. In 1953, Pauling and Corey proposed "rippled β-sheet" modes of H-bond-mediated interstrand assembly for alternating L- and D-peptide strands; this structural hypothesis was complementary to their proposal of "pleated β-sheet" assembly for L-peptides. Although no high-resolution structure has been reported for a rippled β-sheet, there is strong evidence for the occurrence of rippled β-sheets in some racemic peptide assemblies. Here we compare propensities of peptide diastereomers in aqueous solution to form a minimum increment of β-sheet in which two antiparallel strands associate. β-Hairpin folding i2021-01-01T00:00:00Z2021 Sep2025-04-04T09:37:18.046Z2025-04-04T09:37:18.046ZS-EPMC84863513428830510.1002/cbic.202100324