An Exploration of Multiple Component Peptide Assemblies by Enzyme-Instructed Self-Assembly.

ABSTRACT: Based on the motifs (RNISY (M) and DEEVELILGDT (D)) in the protein crystal structures of Merlin and CRL4^DCAF-1, we phosphorylated the tyrosine residue in M and conjugated M to a self-assembling motif to produce a phosphopeptide (1P) and examined enzyme-instructed self-assembly (EISA) of 1P with and without the presence of D (4). Our results show that EISA of 1P forms a hydrogel at exceedingly low volume fraction (~ 0.03%) even with the presence of the hydrophilic peptide, 4. Unlike 1P, 2P (a diastereomer of 1P) or 3P (the enantiomer of 1P) forms a hydrogel via EISA when their concentration is four or three times that of 1P, respectively. Circular dichroism (CD) spectra show that increasing the concentra

SUBMITTER: Shy AN 

PROVIDER: S-EPMC10208383 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature