Fine structural tuning of the assembly of ECM peptide conjugates via slight sequence modifications.

ABSTRACT: The self-assembly of nanostructures from conjugates of elastin-like peptides and collagen-like peptides (ELP-CLP) has been studied as means to produce thermoresponsive, collagen-binding drug delivery vehicles. Motivated by our previous work in which ELP-CLP conjugates successfully self-assembled into vesicles and platelet-like nanostructures, here, we extend our library of ELP-CLP bioconjugates to a series of tryptophan/phenylalanine-containing ELPs and GPO-based CLPs [W₂F _x -b-(GPO) _y ] with various domain lengths to determine the impact of these modifications on the thermoresponsiveness and morphology. The lower transition temperature of the conjugates with longer ELP or CLP domains enables the formation of well-defined nanoparticles

SUBMITTER: Qin J 

PROVIDER: S-EPMC7541060 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature