Syntheses of Enantiopure 1,2-Ethylenediamines with Tethered Secondary Amines of the Formula H2NCH2CH[(CH2) n NHMe]NH2 (n = 1–4) from α-Amino Acids: New Agents for Asymmetric Catalysis

Tris(hydrochloride) adducts of the title compounds­ are prepared from the inexpensive α-amino acids H2N(C=O)CH2CH(NH2)CO2H, HO(C=O)(CH2) n′CH(NH2)CO2H (n′ = 1, 2), and H2N(CH2)4CH(NH2)CO2H, respectively (steps/overall yield = 5/32%, 7/30%, 7/33%, 5/38%). The NH2 group that is remote from the secondary amine is installed via BH3 reduction of an amide [–(C=O)NR2] derived­ from an α-amino carboxylic acid. The MeNHCH2 units are introduced by BH3 reductions of alkyl carbamate [RO(C=O)NHCH2–; R = Et, t-Bu] or amide [MeHN(C=O)–] moieties.

4-Aminoindane Derived Novel Schiff Base Metal Complexes: Synthesis, Characterization, DNA Binding and Molecular Docking Studies

A novel Schiff base [SAL-L=2-((2,3-dihydro-1H-inden-4-ylimino)methyl phenol] was synthesized and used as ligand for the synthesis of Ni(II) and Co(II) complexes. The structural characterization of ligand and its Ni(II) and Co(II) complexes was determined using various spectroscopic methods. Based on spectral studies, a square planar and octahedral geometry have been proposed for Ni(II) and Co(II) complexes, respectively. DNA binding properties of these metal complexes with calf-thymus DNA in tris-hydrochloride buffer (pH 7.2) were investigated using UV- visible absorption studies. The binding constants were in the order of 105 M-1 suggested a good binding affinity towards CT-DNA. The synthesized ligand is docked on TSPO protein showing good binding energy and found to be a potent inhibitor of cancer.

Characterization and intermethod relationships of materials containing purified human pancreatic and salivary amylase.

We describe the preparation and characterization of materials containing human pancreatic and salivary alpha-amylase (EC 3.2.1.1) and examine their relationship to endogenous amylase in human serum. Amylase was purified from human pancreas and saliva by solvent- and salt-fractionation and column chromatography to specific activities of 63 and 279 kU/g, respectively. Four liquid pools, differing only in activity, were prepared from each source of amylase, each in a matrix containing, per liter: 30 g of human albumin, 50 mmol of sodium chloride, 1 mmol of calcium chloride, and 50 mmol of Tris hydrochloride buffer, pH 7.4. Characterization of the pools showed that the amylase activity in the materials was stable for at least six months at 25 degrees C; among-vial variability of amylase activity was less than or equal to 0.5% (2 CV); and the pools were free from eight possible contaminating enzymes. Plots of salivary vs pancreatic amylase activity measure in our materials with eight commercially available methods showed least-squares slopes ranging from 0.51 to 1.0. The intermethod "commutability" of the materials (i.e., how closely they mimic endogenous serum amylase) was examined in relationship to approximately 100 human sera.