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  1. Home
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Browsing by Author "Egelman, Edward H."

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    Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix
    (Springer Nature, 2024) Yu, Le Tracy; Kreutzberger, Mark A. B.; Bui, Thi H.; Hancu, Maria C.; Farsheed, Adam C.; Egelman, Edward H.; Hartgerink, Jeffrey D.; Bioengineering; Chemistry
    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.
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