Enhanced and selective adsorption of cationic dyes using novel biocompatible self-assembled peptide fibrils.

Herein, bio-compatible self-assembled peptide fibrils have been developed for adsorption of organic pollutants for water remediation with high adsorption capacity. The different morphological motifs of self-assembled dipeptide Fmoc-FW-OMe was formulated using solvent modulation which was characterized by optical microscopy, SEM, XRD and FT-IR. Specifically, the fibril structures were used for selective adsorption of cationic dyes from aqueous solutions with exceptional adsorption capacity noted for crystal violet (625 mg/g). To understand the mechanism of dye adsorption, kinetics studies and adsorption isotherm studies were carried out which proved that the adsorption follows second order kinetics and Langmuir adsorption isotherm. The pH studies suggested that the adsorption of dye is much higher in alkaline conditions as compared to acidic conditions. The self-assembled peptide fibrils showed high reusability over five cycles with negligible effect on the dye adsorption capacity. Notably, this is the first report that discusses the application of self-assembled short peptide based fibrils for removal of dyes from waste water and in particular, it demonstrates the highest adsorption capacity reported for crystal violet dye so far. In general, this efficient capturing of dye pollutants with minimum usage of biocompatible adsorbents presents a simple and cost effective method for water remediation.

Stabilized cationic dipeptide capped gold/silver nanohybrids: Towards enhanced antibacterial and antifungal efficacy.

The nanoparticles of silver/gold and cationic peptides have been recognized as potent antimicrobials for long, but their combined effect has so far not been explored. The present study reports the green synthesis of short cationic dipeptide stabilized AuNPs/AgNPs based nanohybrid materials. It thoroughly investigates the effect of conjugation of short cationic peptides on the antimicrobial properties of metallic nanoparticles. In the context of the antimicrobial evaluation of synthesized nanoconjugates, it was observed that peptide capped AgNPs exhibited higher antimicrobial activity as compared to peptide capped AuNPs as well as native peptides and unconjugated metallic nanoparticles. Specifically, l-His-l-Arg-OMe capped AgNPs exhibited MIC of 0.50, 0.37 and 0.25µM against E.coli, S. aureus and S. typhimurium respectively and MIC of 0.80 and 10.00µM against C. albicans and C. glabrata respectively. These results indicate that synthetic dipeptides render AgNPs as better antimicrobial agents in comparison to the native AgNPs and positively charged dipeptides. In addition, the time kill profile of cationic peptide (l-His-l-Arg-OMe) capped AgNPs was found to be even better than the known antibiotics. The cytotoxic behavior of all synthesized nanoconjugates of cationic peptides was studied and was found to be within acceptable limits. The present study opens a completely new class of antimicrobials for combating a wide range of bacterial and fungal pathogens. Another interesting and crucial finding was that dipeptide capped AgNPs displayed maximum antimicrobial activity with observed approximate 2-10 fold reduction in nano formulation dosage against tested microbes.

Self-assembly of aromatic α-amino acids into amyloid inspired nano/micro scaled architects.

In the pursuit for design of novel bio inspired materials, aromatic α-amino acids (phenylalanine, tyrosine, tryptophan and histidine) have been investigated for the generation of well-ordered self-assembled architects such as fibrils, rods, ribbons and twisted nanosheets in varying solvent systems. These nano/micro scaled architects were thoroughly characterized using FE-SEM, confocal microscopy, optical microscopy, 1H NMR, FTIR, XRD and TGA. These self-assembled architects were histologically stained with Congo red and thioflavin T dyes for investigation of amyloid morphology which revealed that the deposited state of ordered assemblies exhibit specific characteristic of amyloid deposits. The self-assembly of aromatic amino acids was observed to be driven by non-covalent forces such as π-π stacking, van der Waals and electrostatic interaction.