Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix

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dc.citation.articleNumber10385en_US
dc.citation.journalTitleNature Communicationsen_US
dc.citation.volumeNumber15en_US
dc.contributor.authorYu, Le Tracyen_US
dc.contributor.authorKreutzberger, Mark A. B.en_US
dc.contributor.authorBui, Thi H.en_US
dc.contributor.authorHancu, Maria C.en_US
dc.contributor.authorFarsheed, Adam C.en_US
dc.contributor.authorEgelman, Edward H.en_US
dc.contributor.authorHartgerink, Jeffrey D.en_US
dc.date.accessioned2025-01-09T20:17:04Zen_US
dc.date.available2025-01-09T20:17:04Zen_US
dc.date.issued2024en_US
dc.description.abstractThe de novo design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II helices, such as those found in collagen, remains relatively limited. In this study, we focus on understanding the sequence-structure relationship in hierarchical assemblies of collagen-like peptides, using defense collagen Surfactant Protein A as a model. By dissecting the sequence derived from Surfactant Protein A and synthesizing short collagen-like peptides, we successfully construct a discrete bundle of hollow triple helices. Amino acid substitution studies pinpoint hydrophobic and charged residues that are critical for oligomer formation. These insights guide the de novo design of collagen-like peptides, resulting in the formation of diverse quaternary structures, including discrete and heterogenous bundled oligomers, two-dimensional nanosheets, and pH-responsive nanoribbons. Our study represents a significant advancement in the understanding and harnessing of collagen higher-order assemblies beyond the triple helix.en_US
dc.identifier.citationYu, L. T., Kreutzberger, M. A. B., Bui, T. H., Hancu, M. C., Farsheed, A. C., Egelman, E. H., & Hartgerink, J. D. (2024). Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix. Nature Communications, 15(1), 10385. https://doi.org/10.1038/s41467-024-54560-zen_US
dc.identifier.digitals41467-024-54560-zen_US
dc.identifier.doihttps://doi.org/10.1038/s41467-024-54560-zen_US
dc.identifier.urihttps://hdl.handle.net/1911/118143en_US
dc.language.isoengen_US
dc.publisherSpringer Natureen_US
dc.rightsExcept where otherwise noted, this work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND) license. Permission to reuse, publish, or reproduce the work beyond the terms of the license or beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.titleExploration of the hierarchical assembly space of collagen-like peptides beyond the triple helixen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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