From Hydrogel to Crystal: A Molecular Design Strategy that Chemically Modifies Racemic Gel-Forming Peptides to Furnish Crystalline Fibrils Stabilized by Parallel Rippled β-Sheets DOI
Tuan D. Samdin, J. Łubkowski, Caleb F. Anderson

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: April 19, 2025

Rippled β-sheets are an underutilized secondary structural motif that hold promise in the rational design of peptide hydrogel materials with unique and desirable properties. Fully capitalizing on potential this element, however, requires a high-resolution molecular understanding interactions they form within supramolecular assemblies comprising material - which absent all reports to date. Herein, we develop strategy modulate phase state β-hairpin peptides prone fibrillar gels into ones assemble crystal lattices, making analysis possible. Truncating, cyclizing Cα-methylating enantiomeric gel-forming affords mirror-image macrocyclic peptides. Crystallography reveals macrocycles coassemble racemic fibril-like unprecedented structure. Extended arrays sheet-rich fibrils contain alternating blocks enantiopure β-hairpins both canonical pleated as well stereocomplexed rippled β-sheets. This structure illuminates new leverage next generation hydrogels provides first crystallographic evidence parallel β-sheet.

Language: Английский

From Hydrogel to Crystal: A Molecular Design Strategy that Chemically Modifies Racemic Gel-Forming Peptides to Furnish Crystalline Fibrils Stabilized by Parallel Rippled β-Sheets DOI
Tuan D. Samdin, J. Łubkowski, Caleb F. Anderson

et al.

Journal of the American Chemical Society, Journal Year: 2025, Volume and Issue: unknown

Published: April 19, 2025

Rippled β-sheets are an underutilized secondary structural motif that hold promise in the rational design of peptide hydrogel materials with unique and desirable properties. Fully capitalizing on potential this element, however, requires a high-resolution molecular understanding interactions they form within supramolecular assemblies comprising material - which absent all reports to date. Herein, we develop strategy modulate phase state β-hairpin peptides prone fibrillar gels into ones assemble crystal lattices, making analysis possible. Truncating, cyclizing Cα-methylating enantiomeric gel-forming affords mirror-image macrocyclic peptides. Crystallography reveals macrocycles coassemble racemic fibril-like unprecedented structure. Extended arrays sheet-rich fibrils contain alternating blocks enantiopure β-hairpins both canonical pleated as well stereocomplexed rippled β-sheets. This structure illuminates new leverage next generation hydrogels provides first crystallographic evidence parallel β-sheet.

Language: Английский

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