Ambient stable solution-processed organic field effect transistors from electron deficient planar aromatics: effect of end-groups on ambient stability.

Ambient stable solution processed n-channel organic field effect transistors (OFETs) are essential for next-generation low-cost organic electronic devices. Several molecular features, such as suitable orbital energy levels, easy synthetic steps, etc., must be considered while designing efficient active layer materials. Here, we report a case of improved ambient stability of solution-processed n-type OFETs upon suitable end-groups substitution of the active layer materials. A pair of core-substituted napthalenediimide (NDIFCN2 and EHNDICN2) derivatives with alkyl and perfluorinated end groups are considered. The transistor devices made out of these two derivatives exhibited largely different ambient stability behavior. The superior device stability (more than 25 days under ambient conditions) of one of the derivatives (NDIFCN2) was ascribed to the presence of fluorinated end groups that function as hydrophobic guard units inhibiting moisture infiltration into the active layer, thereby achieving ambient stability under humid conditions (>65% relative atmospheric humidity). Molecular level optical and electrochemical properties, thermal stability, and the solution-processed (spin coat and drop cast active layers) device characteristics are described in detail. Our findings highlight the requirement of hydrophobic end groups or sidechains for ambient stability of active layer materials, along with deep LUMO levels for ambient stability.

Bicomponent Coassembled Hydrogel as a Template for Selective Enzymatic Generation of DOPA.

In living organisms, tyrosinase selectively produces l-DOPA from l-tyrosine. Here, a bicomponent hydrogel is used as a template for tyrosinase-catalyzed selective generation of l-DOPA from tyrosine. An amphiphilic molecule 1,5-diaminonaphthalene (DAN) coassembles with 1,3,5-benzenetricarboxylic acid (BTC) to form a self-supporting hydrogel. After alteration of complementary acids, DAN does not coassemble to form a hydrogel. The coassembly mechanism is investigated using spectroscopic techniques. The transmission electron microscopy and scanning electron microscopy images reveal the morphology details. The l-DOPA is kept from being oxidized when the hydrogel is used as a template. The enzymatically synthesized l-DOPA can also be separated from the mixture by easy tuning of the bicomponent coassembly.

Tuning the Handedness: Role of Chiral Component in Peptide-Appended Bolaamphiphile-Based Coassembled Hydrogels.

Chirality is the intrinsic property of a molecule that can be tuned by the change in chirality of a molecule or by the addition of a chiral component as an external stimulus. An l-leucine-based dipeptide-appended succinic acid-based bolaamphiphile coassembled with d-tartaric acid to form supramolecular right-handed nanostructured hydrogel, whereas l-tartaric acid coassembled to form supramolecular left-handed nanostructured hydrogel. Scanning electron microscopy and transmission electron microscopy experiments revealed the right- and left-handed helical nanofibers that are responsible for the formation of supramolecular nanostructured hydrogels. The synergistic chiral effect of l-leucine in peptide bolaamphiphile and d/l-tartaric acid plays a significant role in bicomponent gelation with helical nanofibers. The first two amino acids attached to both sides of succinic acid moiety act as a tuning button for supramolecular chirality of amino acids/peptides attached with succinic acid-based bolaamphiphiles. The second amino acid plays the role of modulating supramolecular chirality if the first two amino acids act neutrally to the chirality of bolaamphiphiles, which was confirmed by circular dichroism spectroscopy.

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. The binding mode of the YYY to ds-DNA is elucidated by fluorescence intercalator displacement (FID) assay, melting temperature analysis, viscosity measurement and salt-induced fluorescence quenching study. The studies establish that the YYY recognizes the groove of the ct-DNA. The temperature dependent ITC studies show that the binding interaction is thermodynamically favourable. The compensation between enthalpy and entropy leads to the overall Gibbs free energy change almost invariant. Finally, the generality of the YYY to recognize ds-DNA has been analyzed with other model ds-DNA, ds26, which reveals almost similar binding affinity of the YYY as ct-DNA. The studies elucidate both the spectroscopic and calorimetric insight of the interactions of a homoaromatic tripeptide with ds-DNA and hold the promise of future applications as DNA targeting drug.

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 ß-sheet conformation both in solid and solution. In aqueous solution, FFF self-assembles to form nanostructured aggregates. Interactions of this peptide with calf-thymus DNA (ct-DNA) have been studied using various biophysical techniques including ultraviolet (UV) absorption spectroscopy, fluorescence spectroscopy and circular dichroism (CD) spectroscopy. The value of mean binding constant calculated from UV and fluorescence spectroscopic data is (2.914 ± 0.74) x 103 M-1 which is consistent with an external binding mode. Fluorescence intercalator displacement (FID) assay, iodide quenching study, viscosity measurement and thermal denaturation study of DNA further confirm the groove binding mode of peptide, FFF with ct-DNA. MTT cell survival assay reveals very low cytotoxicity of the peptide toward human lung carcinoma cell line A549.

Controlling Peptide Self-Assembly through a Native Chemical Ligation/Desulfurization Strategy.

Self-assembled peptides were synthesized by using a native chemical ligation (NCL)/desulfurization strategy that maintained the chemical diversity of the self-assembled peptides. Herein, we employed oxo-ester-mediated NCL reactions to incorporate cysteine, a cysteine-based dipeptide, and a sterically hindered unnatural amino acid (penicillamine) into peptides. Self-assembly of the peptides resulted in the formation of self-supporting gels. Microscopy analysis indicated the formation of helical nanofibers, which were responsible for the formation of gel matrices. The self-assembly of the ligated peptides was governed by covalent and non-covalent interactions, as confirmed by FTIR, CD, fluorescence spectroscopy, and MS (ESI) analyses. Peptide disassembly was induced by desulfurization reactions with tris(2-carboxyethyl)phosphine (TCEP) and glutathione at 80 °C. Desulfurization reactions of the ligated peptides converted the Cys and penicillamine functionalities into Ala and Val moieties, respectively. The self-supporting gels showed significant shear-thinning and thixotropic properties.