Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering, and Catalysts in Aldol Reactions.

ABSTRACT: Morphological, spectroscopic, and scattering studies of the self-assembly and aggregation of mixtures of [RF]₄ and P[RF]₄ peptides (where R = arginine; F = phenylalanine; P = proline), in solution and as hydrogels, were performed to obtain information about polymorphism. CD data confirmed a β-sheet secondary structure in aqueous solution, and TEM images revealed nanofibers with diameters of ∼10 nm and micrometer lengths. SAXS curves were fitted using a mass fractal-component and a long cylinder shell form factor for the liquid samples, and only a long cylinder shell form factor for the gels. Increasing the P[RF]₄ content in the systems leads to a reduction in cylinder radius and core scattering density, suggesting an increase in packing of the peptide molec

SUBMITTER: Pelin JNBD 

PROVIDER: S-EPMC7146849 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature