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TitleExploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10385, Year 2024
Publish dateNov 29, 2024
AuthorsLe Tracy Yu / Mark A B Kreutzberger / Thi H Bui / Maria C Hancu / Adam C Farsheed / Edward H Egelman / Jeffrey D Hartgerink /
PubMed 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 ...The 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.
External linksNat Commun / PubMed:39613762 / PubMed Central
MethodsEM (single particle)
Resolution5.0 - 10.2 Å
Structure data

EMDB-44405: Low-resolution cryo-EM structure of the DES-1 collagen-like peptide doublet assembly
Method: EM (single particle) / Resolution: 10.2 Å

EMDB-44406: Cryo-EM structure of the DES-1 collagen-like peptide octadecameric assembly with C6 symmetry
Method: EM (single particle) / Resolution: 5.3 Å

EMDB-44409: Cryo-EM structure of the pentadecameric DES-1 collagen-like assembly
Method: EM (single particle) / Resolution: 5.0 Å

EMDB-44418: Cryo-EM structure of the SPA-human octadecameric collagen-like assembly
Method: EM (single particle) / Resolution: 5.4 Å

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