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

Le Tracy Yu, Mark A. B. Kreutzberger, Thi H. Bui, Maria C. Hancu, Adam C. Farsheed, Edward H. Egelman and Jeffrey D. Hartgerink ()
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Le Tracy Yu: Rice University
Mark A. B. Kreutzberger: University of Virginia School of Medicine
Thi H. Bui: Rice University
Maria C. Hancu: Rice University
Adam C. Farsheed: Rice University
Edward H. Egelman: University of Virginia School of Medicine
Jeffrey D. Hartgerink: Rice University

Nature Communications, 2024, vol. 15, issue 1, 1-11

Abstract: Abstract 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.

Date: 2024
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DOI: 10.1038/s41467-024-54560-z

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