designed aliphatic and aromatic peptides assemble into amyloid-like cytotoxic supramolecular nanofibrils.

Peptides are very interesting biomolecules that upon self-association form a variety of thermodynamically stable supramolecular structures of nanometric dimension nanotubes, nanorods, nanovesicles, nanofibrils, nanowires and many others. Herein, we report six peptide molecules having a general chemical structure, H-Gaba-X-X-OH (Gaba: γ-aminobutyric acid, X: amino acid). Out of these six peptides, three are aromatic and the others are aliphatic.

Poly C Binding Protein 2 dependent nuclear retention of the utrophin-A mRNA in C2C12 cells.

Upregulation of utrophin, the autosomal homologue of dystrophin, can compensate dystrophin deficiency in Duchenne Muscular Dystrophy (DMD) although the therapeutic success is yet to be achieved. The present study has identified Poly (C) binding protein 2 (PCBP2) as a post-transcriptional suppresser for the expression of utrophin-A, the muscle-specific utrophin isoform. This study confirms nuclear retention of utrophin-A mRNA in C2C12 cells, which is mediated by PCBP2.

Ecological safety with multifunctional applications of biogenic mono and bimetallic (Au-Ag) alloy nanoparticles.

Recently, the design and biosynthesis of metallic nanoparticles (NPs) have drawn immense interest, but their very specific function and secondary toxic effects are major concern towards commercial application of NPs. That's why environment-friendly (nontoxic) NPs having multiple functions are extremely important. Herein, we report the mechanism of biosynthesis of mono and bimetallic (Au-Ag) alloy NPs and study their multifunctional (antioxidant, antifungal and catalytic) activity and ecotoxicological property.

Targeting G-quadruplex DNA with synthetic dendritic peptide: modulation of the proliferation of human cancer cells.

Telomerase, a reverse transcriptase enzyme, is found to over express in most cancer cells. It elongates the telomere region by repeated adding of TTAGGG in the 3'-end and leads to excess cell proliferation which causes cancer. G-quadruplex (G4) formation can inhibit such telomere lengthening.

Author Correction: Process optimization for biosynthesis of mono and bimetallic alloy nanoparticle catalysts for degradation of dyes in individual and ternary mixture.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Process optimization for biosynthesis of mono and bimetallic alloy nanoparticle catalysts for degradation of dyes in individual and ternary mixture.

Nanoparticle (NP) catalysts are widely used for removal of dyes for single use, but there is an acute need for developing catalysts with high efficiency and reusability for mixed dyes. Here we first optimized the process (reactant proportion, temperature, time, and pH) for biosynthesis of monometallic Ag, Au and bimetallic Au-Ag alloy NP catalysts using Polyalthia longifolia leaf extract. The biosynthesized NP catalysts were characterized by UV-vis, DLS, Zeta potential, TEM and EDX study while the probable biomolecules responsible for biosynthesis were identified by FTIR and GC-MS/MS analysis.

Engineering of Supramolecular β-Sheet and Nontoxic Amyloid Fibrils from Synthetic Oligopeptides Containing γ-Aminobutyric Acid as the N-Terminal Residue.

Here we demonstrate that three synthetic tripeptides containing conformationally flexible γ-aminobutyric acid (γ-Abu) as the N-terminal residue form supramolecular β-sheet and nanofibrillar aggregates upon self-association in aqueous medium. Congo red and thioflavin T binding study establish that these nanofibrillar aggregates are amyloidogenic in nature. The MTT cell survival assay suggests that these amyloid-like nanofibrillar aggregates are nontoxic toward cultured Neuro 2A cells.

Molecular recognition of double-stranded DNA by a synthetic, homoaromatic tripeptide (YYY): The spectroscopic and calorimetric study.

The intermolecular interactions of a homoaromatic tripeptide, H-Tyr-Tyr-Tyr-OH (YYY) with model double-stranded (ds) DNA (ct-DNA) have been investigated by isothermal titration calorimetric (ITC) method along with various biophysical techniques such as fluorescence, time correlated single photon counting (TCSPC) and circular dichroism (CD) spectroscopy. The binding affinity [log (K) at 25 °C] of the YYY to ct-DNA is calculated as ≈4.3.

Insight into the binding of a non-toxic, self-assembling aromatic tripeptide with ct-DNA: Spectroscopic and viscositic studies.

The report describes the synthesis, self-association and DNA binding studies of an aromatic tripeptide H-Phe-Phe-Phe-OH (FFF). The peptide backbone adopts β-sheet conformation both in solid and solution. In aqueous solution, FFF self-assembles to form nanostructured aggregates.

Conformational analysis of an acyclic tetrapeptide: ab-initio structure determination from X-ray powder diffraction, Hirshfeld surface analysis and electronic structure.

A terminally protected acyclic tetrapeptide has been synthesized, and the crystal structure of its hydrated form, Boc-Tyr-Aib-Tyr-Ile-OMe·2H2O (1), has been determined directly from powder X-ray diffraction data. The backbone conformation of tetrapeptide (1) exhibiting two consecutive β-turns is stabilized by two 4 → 1 intramolecular N-H · · · O hydrogen bonds. In the crystalline state, the tetrapeptide molecules are assembled through water-mediated O-H · · · O hydrogen bonds to form two-dimensional molecular sheets, which are further linked by intermolecular C-H · · · O hydrogen bonds into a three-dimensional supramolecular framework.

Self-assembling dipeptide-based nontoxic vesicles as carriers for drugs and other biologically important molecules.

Self-assembling short peptides can offer an opportunity to make useful nano-/microstructures that find potential application in drug delivery. We report here the formation of multivesicular structures from self-assembling water-soluble synthetic amphiphilic dipeptides containing a glutamic acid residue at the C-terminus. These vesicular structures are stable over a wide range of pH (pH 2-12).

Concentration dependent transformation of oligopeptide based nanovesicles to nanotubes and an application of nanovesicles.

The concentration dependent transformation of an oligopeptide nanostructure from nanovesicles to nanotubes at neutral pH is presented. The oligopeptide Acp-Tyr-Glu (Acp: 6-aminohexanoic acid) forms nanovesicles at a concentration of 6.9 mg mL(-1).

Tetrapeptide-based hydrogels: for encapsulation and slow release of an anticancer drug at physiological pH.

Here, we report two synthetic oligopeptide-based, thermoreversible, pH-sensitive hydrogels. In gel phase, these self-assembling tetrapeptides form a long interconnected nanofibrilar network structure, as is evident from various microscopic techniques, including field emission scanning electron microscopy (FE-SEM), transmission electron microscopy (TEM), and atomic force microscopy (AFM). FTIR, circular dichroism, and wide angle X-ray diffraction (WAXD) favor an antiparallel beta-sheet structure of these gelators in the gel state.

Water-soluble tripeptide Abeta (9-11) forms amyloid-like fibrils and exhibits neurotoxicity.

A water-soluble, hydrophilic tripeptide GYE, having sequence identity with the N-terminal segment of amyloid peptides Abeta(9-11), upon self-association exhibits amyloid-like fibrils and significant neurotoxicity towards the Neuro2A cell line. However, the tripeptides GFE and GWE, in which the centrally located tyrosine residue has been replaced by phenylalanine or tryptophan, fail to show amyloidogenic behavior and exhibit little or no neurotoxicity.