Unusual Aggregates Formed by the Self-Assembly of Proline, Hydroxyproline, and Lysine

There is a plethora of significant research that illustrates toxic self-assemblies formed by the aggregation single amino acids, such as phenylalanine, tyrosine, tryptophan, cysteine, and methionine, their implication on etiology inborn errors metabolisms (IEMs), phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria, hypermethioninemia, respectively. Hence, studying behavior acids very crucial from chemical neuroscience perspective to understanding common between acid metabolite disorders amyloid diseases like Alzheimer’s Parkinson’s. Herein we report properties nonaromatic l-proline (Pro), l-hydroxyproline (Hyp), l-lysine hydrochloride (Lys). The morphologies self-assembled structures Pro, Hyp, Lys were extensively studied various microscopic techniques, controlled morphological transitions observed under varied concentrations aging times. mechanism structure formation was deciphered concentration-dependent 1H NMR analysis, which revealed role hydrogen bonding hydrophobic interactions in Lys. MTT assays neural (SHSY5Y) cell lines aggregates reduced viability dose-dependent manner. These results may have important implications patho-physiology hyperprolinemia, hyperhydroxyprolinemia, hyperlysinemia since all these IEMs are associated with severe neurodegenerative symptoms, including intellectual disability, seizures, psychiatric problems. Our future studies will endeavor study biomolecular assemblies greater detail immuno-histochemical analysis advanced biophysical assays.