Rational and controllable syntheses of variants of modified N-confused N-fused porphodimethenes and a porphotrimethene with adaptive properties.

Retrosynthetic design and synthesis with structural isolation of two unprecedented core modified N-confused N-fused porphodimethene-like porphyrinoids possessing a [5.5.5.5] tetracyclic ring with tunable photophysical properties is reported. The solid-state X-ray crystal structure reveals the expected cis geometry for the meso-sp3 carbons. Controlled chemical oxidation of the porphodimethene analogue 11 bearing the N-confused pyrrole moiety to the corresponding porphotrimethene 12 has been achieved in quantitative yield, while 10 bearing the N-methyl N-confused pyrrole moiety remained unsusceptible to chemical oxidation. All three S2N3 hybrid N-confused N-fused porphodi(tri)methene-like porphyrinoids 10-12 could recognize the fluoride anion with high selectivity; however, porphodimethene 10 and porphotrimethene 12 do so via deprotonation rather than an anion recognition based mechanism as has been anticipated in the case of porphodimethene 11.

NIR Absorbing Aromatic E-Ethylene Bridged Hexaphyrins (2.1.1.2.1.1): Synthesis, Characterization, and Protonation Studies.

Judicious syntheses, spectroscopic analyses, and solid state structural evidence of two structural variants (with planar geometry) of strongly aromatic hybrid [30] E-ethylene bridged hexaphyrins (2.1.1.2.1.1) exhibiting strong NIR absorption are reported. The induced correspondence of fused phenanthrene on the pyrrole moieties has led to a further red-shift of up to ∼45 nm in the neutral and protonated form of the macrocycles. The electronic nature and aromaticity of both hexaphyrins are fully supported by DFT calculations.

Tailor-made aromatic porphyrinoids with NIR absorption.

The highlight of this article is the recent progress in the state-of-the-art synthetic design and isolation of artificial porphyrinoids by swapping pyrrole component(s) with diverse functionalized pyrrolic(heterocyclic)/carbacycle building block(s) to compare the impact on the electronic absorption spectra and aromaticity of the incorporated isomeric/expanded porphyrinoids. Attention has been directed towards five distinct criteria of utilizing functionalized pyrrolic(heterocyclic)/aromatic hydrocarbons as synthons for NIR absorbing aromatic isomeric (N-confusion)/expanded porphyrinoids (with five/six heterocycles): (i) fused or annelated pyrrole (heterocycle), (ii) functionalized bi-pyrrole/bi-thiophene/bi-furan building blocks, (iii) azulene based carbacycle building block, (iv) vinylogous aromatic carbacycle/heterocycle(s) building block and (v) N-confused pyrrole ring(s), and N-confused fused pyrrole ring(s) leading to π-extension. These hybrid porphyrinoids are ideal candidates for basic research into macrocyclic aromaticity and for many potential applications owing to NIR absorption.

Structural isolation of NIR absorbing ferrocenyl bridged N-confused fused expanded phlorin, N-confused porphodimethene and the π-extended corrorin isomer: synthesis and characterization.

Concise syntheses and spectroscopic, solid state X-ray crystal structure and theoretical studies of three electronically appealing new generation hitherto unknown ferrocenyl bridged N-confused heterocyclic macrocycles with (without) fusion are reported. Intriguingly, the expanded N-confused fused phlorin (1.1.1.1.1) with the built-in tripentacyclic [5.5.5] moiety exhibits tailing of the NIR absorption band beyond 1000 nm while the nonconjugated porphodimethene and a new generation π-extended isomeric corrorin analogue exhibit UV-vis absorption.

Targeted synthesis of meso-aryl substituted aromatic trans-doubly N-confused dithia/diselena [18] porphyrins (1.1.1.1) with NIR absorption: spectroscopic and theoretical characterization.

High yield synthesis and spectroscopic isolation of two hitherto unknown highly stable single conformers of meso-aryl substituted dithia/diselena trans-doubly N-confused porphyrins with fully π-conjugated [18] annulene structures are reported. In-depth solution state spectroscopic measurements and DFT level theoretical calculations strongly show the distinct aromaticity with strong NIR absorption of these new macrocycles.

Purification and Characterization of Natural Solid-Substrate Degrading and Alcohol Producing Hyperthermostable Alkaline Amylase from Bacillus cereus (sm-sr14).

OBJECTIVE: Amylases enzymes hydrolyze starch molecules to produce diverse products including dextrins, and progressively smaller polymers. These include glucose units linked through α-1- 1, α-1-4, α-1-6, glycosidic bonds. METHODS: This enzyme carrying an (α /ß) 8 or TIM barrel structure is also produced containing the catalytic site residues. These groups of enzymes possess four conserved regions in their primary sequence. In the Carbohydrate-Degrading Enzyme (CAZy) database, α-amylases are classified into different Glycoside Hydrolase Families (GHF) based on their amino acid sequence. The present objective was to study one such enzyme based on its molecular characterization after purification in our laboratory. Its main property of solid-natural starch degradation was extensively investigated for its pharmaceutical/ industrial applications. RESULTS: Amylase producing bacteria Bacillus cereus sm-sr14 (Accession no. KM251578.1) was purified to homogeneity on a Seralose 6B-150 gel-matrix and gave a single peak during HPLC. MALDITOF mass-spectrometry with bioinformatics studies revealed its significant similarity to α/ß hydrolase family. The enzyme showed an efficient application; favourable Km, Vmax and Kcat during the catalysis of different natural solid starch materials. Analysis for hydrolytic product showed that this enzyme can be classified as the exo-amylase asit produced a significant amount of glucose. CONCLUSION: Besides the purified enzyme, the present organism Bacillus cereus sm-sr14 could degrade natural solid starch materials like potato and rice up to the application level in the pharmaceutical/ industrial field for alcohol production.

Conformational-Switch Based Strategy Triggered by [18] π Heteroannulenes toward Reduction of Alpha Synuclein Oligomer Toxicity.

A water-soluble meso-carboxy aryl substituted [18] heteroannulene (porphyrin) and its Zn-complex have been found to be viable in targeting α-Syn aggregation at all its key microevents, namely, primary nucleation, fibril elongation, and secondary nucleation, by converting the highly heterogeneous and cytotoxic aggresome into a homogeneous population of minimally toxic off-pathway oligomers, that remained unexplored until recently. With the EC50 and dissociation constants in the low micromolar range, these heteroannulenes induce a switch in the secondary structure of toxic prefibrillar on-pathway oligomers of α-Syn, converting them into minimally toxic nonseeding off-pathway oligomers. The inhibition of the aggregation and the reduction of toxicity have been studied in vitro as well as inside neuroblastoma cells.

The Dual Carboxymethyl Cellulase and Gelatinase Activities of a Newly Isolated Protein from Brevibacillus agri ST15c10 Confer Reciprocal Regulations in Substrate Utilization.

A protein showing endoglucanase-peptidase activity was prepared from a newly isolated bacterium (ST15c10). We identified ST15c10 as Brevibacillus agri based on electron-microscopic images and its 16S-rDNA sequence (GenBank accession No. HM446043), which exhibits 98.9% sequence identity to B. agri (KZ17)/B. formosus (DSM-9885T)/B. brevis. The enzyme was purified to homogeneity and gave a single peak during high-performance liquid chromatography on a Seralose 6B-150 gel-matrix/C-18 column. MALDI-TOF mass-spectrometry and bioinformatics studies revealed significant similarity to M42-aminopeptidases/endoglucanases of the CelM family. These enzymes are found in all Brevibacillus strains for which the genome sequence is known. ST15c10 grows optimally on carboxymethyl cellulose (CMC)-gelatin (40°C/pH 8-9), and also shows strong growth/carboxymethyl cellulase (CMCase) activity in submerged bagasse fermentation. The purified enzyme also functions as endoglucanase with solid bagasse/rice straw. Its CMCase activity (optimal at pH 5.6 and 60°C/Km = 35.5 µM/Vmax = 1,024U) was visualized by zymography on a CMC-polyacrylamide gel, which provided a strong band of approximately 70 kDa. The purified enzyme also showed strong peptidase (gelatinase) activity (pH 7.2/40°C during zymography on 6-12% gelatin/1% gelatin-PAGE (at approx. 70 kDa). The CMCase activity is inhibited by the metal ions Mn/Cu/Fe/Co (50%), Hg/KMnO4 (100%), and by glucose or lactose (50-75%; all at 1 mM). The observed dose/time-dependent inhibition by Hg ions could be prevented with 2-mercaptoethanol. A comparison of the B. agri endoglucanase-aminopeptidase (ELK43520; 350 aa) with other members of the M42-family revealed the conservation of active-site residues Cys256/Cys260, which were previously identified as metal-binding sites. Regulation of the endoglucanase activity probably occurs via metal binding-triggered changes in the redox state of the enzyme. Studies on this type of enzyme are of high importance for basic scientific and industrial research.