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

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 col

SUBMITTER: Yu LT 

PROVIDER: S-EPMC11606958 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature