Organic derivatives of aluminium. Part I. Reactions of alkanolamines with aluminium isopropoxide

Reactions of alkanolamines [R₁R₂NXOH; R₁ = H, CH₃, C₂H₅; R₂ = H, CH₃, C₂H₅ and X = -CH₂CH₂-, -CH₂CH₂CH₂-, -CH₂CHCH₃, -C₆H₄CH₂CH₂-] with aluminium isopropoxide in different molar ratios (1 to 3) yield compounds of the type Al(OPrⁱ)_3?n(OXNR₁R₂)_n, where ‘n’ can be 1, 2 and 3. Most of the derivatives are distillable liquids, soluble in common organic solvents and susceptible to hydrolysis even by atmospheric moisture. The new derivatives are characterized by elemental analysis, IR and ¹H NMR spectra. Molecular weight measurements of Al(OPrⁱ)_3?n(OXNR₁R₂)_n reveal them to be tetrameric in nature.     

Obtaining high transesterification activity for subtilisin in ionic liquids

It is known that subtilisin shows poor transesterification activity in ionic liquids (ILs). The present work, taking subtilisin as the system, explores approaches for biocatalyst preparations, which are capable of yielding higher/adequate transesterification activity in these solvents. Of all the approaches tried, enzyme precipitated and rinsed with n-propanol (EPRP) gave the best results (about 10,000 times increase in initial rates in 1-butyl-3-methylimidazolium hexafluorophosphate ([Bmim][PF(6)]) over what is obtained with pH tuned lyophilized powders). In case of water soluble ionic liquid 1-butyl-3-methylimidazolium tetrafluoroborate ([Bmim][BF(4)]), pH tuned lyophilized subtilisin did not show any transesterification activity. EPRP, however, gave an initial rate (for transesterification) of 2.78 mmol mg(-1) h(-1).     

IR investigation on dehydrophenylalanine containing model peptides in helical conformation deposited on a crystal surface

Fourier transform ir spectra have been recorded for three 3₁₀‐helical and one α‐helical pentapeptides containing dehydrophenylalanine, in a thin solid film, in order to find marker bands for various secondary structures encountered in peptides containing dehydroaminoacids. The peptide solutions were deposited and dried as thin film on zinc selenide crystal surface. This convenient sampling method has provided reliable estimates of peptide secondary structure in solid state. Detailed vibrational assignments in the spectral region between 1200–1700 cm⁻¹ are reported. In this region, peptide amide I, II, and III vibrations occur. Spectra–structure correlation has been presented based on the amide modes. Comparison of the ir spectra with available crystal structure data provides qualitative support for assignments of ir bands to 3₁₀‐helical structure and α‐helical structure in dehydrophenylalanine containing pentapeptides. Band frequency assignments for 3₁₀‐helical conformation are consistent for all three peptides. All the assignments agree closely with the theoretical predictions. The spectral differences between 3₁₀‐helical peptides and the α‐helical peptide have been highlighted. These findings demonstrate that a method based on ir spectroscopy can be developed for a useful approximation of three‐dimensional structure of dehydropeptides in solid state. © 1999 John Wiley & Sons, Inc. Biopoly 50: 595–601, 1999     

Efficient and Stable Tin–Lead Perovskite Photoconversion Devices Using Dual-Functional Cathode Interlayer

Tin–lead halide perovskites (TLHPs) are promising photoactive materials for photovoltaics (PVs) due to reduced toxicity and broad light absorption. However, their inherent ionic vacancies facilitate inward metal diffusion, accelerating device degradation. Here, efficient, stable TLHP-based PV and photoelectrochemical (PEC) devices are reported containing a chemically protective cathode interlayer—amine-functionalized perylene diimide (PDINN). Solution-processed PDINN effectively extract electrons and suppress inward-metal diffusion by forming tridentate metal complexes with its nucleophilic sites. The PV device achieved an efficiency of 23.21% (>81% retention after 750 h at 60 °C and >90% retention after 3100 h at 23 ± 4 °C), and the first demonstration of TLHP-based PEC devices exhibit a record-high bias-free solar hydrogen production rate (33.0 mA cm⁻²; ≈3.42 × 10⁻⁶ kg s⁻¹ m⁻²) when coupled with biomass oxidation, which is ≈1.7-fold higher than the ultimate target set by the U.S. Department of Energy for one-sun hydrogen production. These findings demonstrate the potential of TLHPs for efficient, stable photoconversion by the molecular design of the cathode interlayer.     

Molecular cloning and characterization of Brugia malayi hexokinase

5' EST from filarial gene database has been subjected to 3' rapid amplification of cDNA ends (RACE), semi-nested PCR and PCR to obtain full-length cDNA of Brugia malayi. Full-length hexokinase gene was obtained from cDNA using gene specific primers. The elicited PCR product was cloned, sequenced and expressed as an active enzyme in Escherichia coli. Sequence analysis of B. malayi hexokinase (BmHk) revealed 59% identity with nematode Caenorhabditis elegans but low similarity with all other available hexokinases including human. BmHk, an apparent tetramer with subunit molecular mass of 72 kDa, was able to phosphorylate glucose, fructose, mannose, maltose and galactose. The Km values for glucose, fructose and ATP were found to be 0.035+/-0.005, 75+/-0.3 and 1.09+/-0.5 mM respectively. BmHk was strongly inhibited by ADP, glucosamine, N-acetyl glucosamine and mannoheptulose. The recombinant enzyme was found to be activated by glucose-6-phosphate. ADP exhibited noncompetitive inhibition with the substrate glucose (Ki=0.55 mM) while, mixed type of inhibition was observed with inorganic pyrophosphate (PPi) when ATP was used as substrate (Ki=9.92 microM). The enzyme activity is highly dependent on maintenance of free sulfhydryl groups. CD analysis indicated that BmHk is composed of 37% alpha-helices and 26% beta-sheets. The observed differences in kinetic properties of BmHk as compared to host enzyme may facilitate designing of specific inhibitors against BmHk.     

Characterization of the post-translational modification of recombinant human BMP-15 mature protein

Bone morphogenetic protein-15 (BMP-15) is an oocyte-secreted factor critical for the regulation of ovarian physiology. When recombinant human BMP-15 (rhBMP-15) produced in human embryonic kidney 293 cells was subjected to SDS-PAGE analysis, two mature protein forms corresponding to 16 kDa (P16) and 17 kDa (P17) were observed. Despite the physiological relevance and critical function of BMP-15 in female reproduction, little is known about the structure of rhBMP-15. Here, we have analyzed the structure of the rhBMP-15 mature proteins (P16 and P17) using state-of-the-art proteomics technology. Our findings are as follows: (1) the N-terminal amino acid of P16 and P17 is pyroglutamic acid; (2) the Ser residue at the sixth position of P16 is phosphorylated; (3) P17 is O-glycosylated at Thr10; and (4) the C-terminal amino acid of P16 and P17 is truncated. These findings are the first knowledge of the structure of rhBMP-15 mature protein toward understanding the molecular basis of BMP-15 function and could provide an important contribution to the rapidly progressing research area involving oocyte-specific growth factors in modulation of female fertility.