Self-assembly of l-phenylalanine amino acid: electrostatic induced hindrance of fibril formation.

ABSTRACT: Nanostructure morphology originating from the self-assembly of molecules has attracted substantial attention due to its role in toxic amyloid fibril formation and immense potential in the design and fabrication of novel biomaterials. This study presents the role of intermolecular electrostatic interaction on the self-assembly process of l-phenylalanine (L-Phe) amino acid. We have employed attenuated total reflection Fourier transform infrared spectroscopy to probe the existence of different ionization states of the amino acid in various pH aqueous solutions. The self-assembly process of L-Phe in the aqueous phase is explored by using circular dichroism absorption and nuclear magnetic resonance spectroscopic tools. The observed spectral features have shown the signature of higher order stru

SUBMITTER: Tomar D 

PROVIDER: S-EPMC9063664 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature