Structural and Positional Effects of Peptoid Residues on Triple Helix Stability
)-N-(1-phenylethyl)-Gly (Nspe) stabilized the triple helix better than all other residues except Hyp through newly discovered intrachain CH···π interactions. This research deepens our understanding of triple helical folding and introduces new strategies for designing stable collagen mimetic peptides with diverse side chains, expanding potential applications in biomedicine and biomaterials.
Authors
- S. Michael Yu (ORCID: https://orcid.org/0000-0002-5171-2644)
- Julian L. Kessler (ORCID: https://orcid.org/0000-0002-4497-235X)
- Frank G. Whitby (ORCID: https://orcid.org/0000-0003-3511-2216)
- Kent Kirshenbaum (ORCID: https://orcid.org/0000-0003-0426-2772)
- Dana E. Katz
- Pahweenvaj Ratnatilaka Na Bhuket (ORCID: https://orcid.org/0000-0001-9506-4477)
- James R. B. Eastwood (ORCID: https://orcid.org/0000-0003-3895-5227)
- Christopher P. Hill (ORCID: https://orcid.org/0000-0001-6796-7740)
- Zhao Qin
Institutions
- Xinjiang Medical University (CN)
- Sun Yat-sen University (CN)
- University of Utah (US)
- Fifth Affiliated Hospital of Xinjiang Medical University (CN)
- Department of Physics, Mathematics and Informatics (BY)
- New York University (US)
- Syracuse University (US)
- Dubai Pharmacy College (AE)
Publication Details
- Journal
- Biomacromolecules
- Published
- 2026-04-03
- DOI
- https://doi.org/10.1021/acs.biomac.5c02232
- Primary Topic
- Chemical Synthesis and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- NIH Office of the Director
- National Institute of General Medical Sciences
- National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Basic Energy Sciences
- Office of Research Infrastructure Programs, National Institutes of Health
- Argonne National Laboratory