Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres.

ABSTRACT: The development of novel strategies to construct collagen mimetic peptides capable of self-assembling into higher-order structures plays a critical role in the discovery of functional biomaterials. We herein report the construction of a novel type of amphiphile-like peptide conjugating the repetitive triple helical (GPO) _m sequences characteristic of collagen with terminal hydrophilic aspartic acids. The amphiphile-like collagen mimic peptides containing a variable length of (Gly-Pro-Hyp) _m sequences consistently generate well-ordered nanospherical supramolecular structures. The C-terminal aspartic acids have been revealed to play a determinant role in the appropriate self-assembly of amphiphile-like collagen mimic peptides. Their presence is a prerequis

SUBMITTER: Yao L 

PROVIDER: S-EPMC9077330 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature