Self-assembled peptide nanostructures have been increasingly exploited as functional
materials for applications in biomedicine and energy. The emergent properties of these …

Noncovalent interactions are the main driving force in the folding of proteins into a 3D
functional structure. Motivated by the wish to reveal the mechanisms of the associated self …

Dipeptides are highly attractive because they are biocompatible building blocks and can be
manipulated to form various sensing materials through molecular assembly. These sensors …

The difference in the crystal structure and growth kinetics of microtubes formed from l-and d-
enantiomers of diphenylalanine dipeptide is investigated both experimentally and …

UV irradiation of aligned diphenylalanine peptide nanotubes (FF-PNTs) decorated with
plasmonic silver nanoparticles (Ag NPs) enables photo-induced surface-enhanced Raman …

The natural ability of peptides and proteins to self-assemble into elongated fibrils is
associated with several neurogenerative diseases. Diphenylalanine (FF) tubular structures …

The elastic properties of the nanotubes of self-assembled aromatic dipeptide
diphenylalanine are investigated by means of Raman spectroscopy and a mass-in-mass 1D …

The structure and properties of diphenylalanine (FF) peptide nanotubes (PNT) based on
phenylalanine were investigated by various molecular modeling methods. The main …

The self-assembling of small peptides not only leads to the formation of intriguing
nanoarchitectures, but also generates materials with unexpected functional properties …

The chirality quantification is of great importance in structural biology, where the differences
in proteins twisting can provide essentially different physiological effects. However, this …