Alanine‐Induced Alteration of Organogelation Properties of Phenylalanine‐Based Shortest Peptide Sequence

Abstract

AbstractShort peptide based Low‐molecular‐weight‐organogelators (LMWGs), or supramolecular gels have recently gained large attention due to their enormous application in several biophysical and biochemical contexts. Out of the 20 naturally occurring amino acids Phenylalanine (Phe) acts as a good organogelators. Biophysical parameters like heat, pH, and solvent polarity, along with light, ultrasound, ions, can affect in alteration of supramolecular self‐aggregation at the molecular level in moderate length of peptide sequences; however, we focused here on how the conformational characteristics and supramolecular assemblages of the excellent LMWG Phe would be influenced by its substitution with similar hydrophobic amino acids (e.g Ala) in the same organic solvent even in the shortest two residue sequence. Using different microscopic and biophysical techniques, it is observed that the supreme capability of Phe residue as LMWG in the formation of supramolecular self‐aggregation in Hex‐Phe(1)‐Phe(2)‐OMe (FF) in organic solvents has been completely altered from fibrillary dendrimeric network to the crystalline phase by substitution with Ala at the C‐terminal [Hex‐Phe(1)‐Ala(2)‐OMe](FA) in a simple two residue sequence. This demonstrates unequivocally how a little change in the peptide side chain has the unique ability to form a distinct 3D supramolecular assembly and establishes the context‐dependent supramolecular morphology of the peptide‐based LMWG.