The peptide based super-gelators are highly soluble in non-toxic organic solvent ethanol, the solution is easy to handle and just by spraying the ethanol solution over an oil–water mixture it is able to form an organogel at room temperature.
Aggregation of proteins and peptides into fibrils are associated with many neurodegenerative disease of human, including Alzheimer’s disease, Parkinson’s disease and non-neurological type-II diabetes. Better understanding of the fibril formation...
The effect of geometrically rigid
trans α,β-unsaturated
ε-amino acids on the structure, folding, and assembly of α,ε-hybrid
peptide foldamers has been reported. From single-crystal diffraction
analysis, the unsaturated tetrapeptide
1
has stapler-pin-like
structure but without intramolecular hydrogen bond. The asymmetric
unit has two molecules that are stabilized by multiple intermolecular
hydrogen bonding interactions as well as π–π stacking
interactions between the aromatic rings of 3-aminocinnamic acid. Peptide
1
does not form organogel. But on hydrogenation, peptide
1
provides the saturated α,ε-hybrid peptide foldamer
2
, which forms instant gel in most of the aromatic solvents.
The gel exhibits high stability. The unsaturated peptide
1
has porous microsphere morphology, but saturated analogue
2
has ribbonlike morphology. The gel has been used efficiently
for removal of cationic organic pollutants from waste water.
The development of engineered hybrid systems by encapsulating nanoparticles in gel scaffolds and their synergistic effects are highly crucial for the fabrication of advanced functional materials. Herein, a series of dipeptides containing an aromatic amino acid at the N-terminal and an aliphatic amino acid at the C-terminal were synthesized and studied. Among them, only the dipeptide L-Phe-L-Val can form both hydro-and organogelator, depending on the N-and C-terminal protecting groups. The organogel shows bright blue emission under 366 nm UV irradiation; however, the hydrogel does not show such blue emission. Such kind of emission may be due to the self-assembly and high degree of aggregation in the gel state of the phenyl ring. The blue-emitting organogel efficiently encapsulates green emission source CdSe quantum dots and red emission source LD 700 perchlorate dye. The resulting organic− inorganic hybrid gel exhibits white light emission due to the synergistic effect under 366 nm UV irradiation.
An α–α corner mimetic self-assembles into a rod shape supramolecular structure which bends and closes end-to-end like a cyclization reaction to form toroids.
The dipeptides 1–4 with a triazole containing synthetic amino acid and Leu/ Phe/ Val/ Gly have been designed and synthesized as a potent antileishmanial agent. The 1‐(2‐Amino‐phenyl)‐1H‐[1, 2,3] triazole‐4‐carboxylic acid was synthesized using click chemistry approach. From X‐ray crystallography, the peptide 1 containing a Leu residue at C‐terminus adopts kink like structure but there is no intramolecular hydrogen bond. So, the hydrogen bonding sites are free and allowed for intermolecular interaction with the guests. The phenylalanine analogue 2 where the phenyl and triazole rings are perpendicular to each other also form supramolecular column‐like structure through π‐π stacking interaction. The incorporation of a triazole containing synthetic amino acid at the N‐terminus enhances its anti‐parasites activity. The properties such as lipophilicity and cytotoxicity, are relevant factors for the design of new antileishmanial agent. IC50 value were calculated for dipeptides 1–4 using normal growth inhibition strategy. For dipeptide 1, IC50 value is 11μg/ml and the Phe containing dipeptide 2 exhibits IC50 21.17μg/ml on Leishmania major promastigotes. But the Val and Gly containing dipeptides 3 and 4 have IC50 values 138.23 μg/ml and 21.75 μg/ml respectively. The higher lipophilicity of dipeptide 1 is likely to improve the chances of reaching this intracellular parasite. The experimental result show that the triazole‐based dipeptide 1 is promising as antileishmanial agent.
The crystal plasticity, due to bromine–bromine interactions, plays a crucial role in generating a slip plane and thus, under mechanical force, crystals undergo bending without affecting their fluorescent properties.
A simple
and cost-effective peptide-based in-field detection of
the nitro explosive 2,4,6-trinitrophenol (TNP) in the solution, solid,
and vapor state at very low concentration has been developed. In solution,
the peptide experiences huge fluorescence quenching even at the ppb
level concentration of TNP. The fluorescence turn-off process is governed
by the charge transfer complex formation with TNP, almost immediately.
Moreover, the probe exhibits very high selectivity and low interference
of other analogues nitro explosives toward the detection of TNP. The
detection can be done in-field at any condition such as in the solution
state, solid state, as well as vapor state with a paper strip device
and can be observed by the naked eye, which is necessary for a real-time
explosive detector without any sophisticated and expensive instruments
with a quicker response time.
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