muramidase and 1-2-cyclohexanediamine

muramidase has been researched along with 1-2-cyclohexanediamine* in 3 studies

Other Studies

3 other study(ies) available for muramidase and 1-2-cyclohexanediamine

ArticleYear
Fluorescence Behavior of Schiff Base-N, N'-bis(salicylidene) Trans 1, 2-Diaminocyclohexane in Proteinous and Micellar Environments.
    Journal of fluorescence, 2017, Volume: 27, Issue:6

    Fluorescence properties of N, N'-bis(salicylidene) trans 1, 2-diaminocyclohexane (H

    Topics: Animals; Cattle; Cyclohexylamines; Fluorescence; Fluorescent Dyes; Humans; Micelles; Muramidase; Salicylates; Schiff Bases; Serum Albumin; Spectrometry, Fluorescence; Surface-Active Agents

2017
Synthesis, characterization and theoretical calculations of (1,2-diaminocyclohexane)(1,3-diaminopropane)gold(III) chloride complexes: in vitro cytotoxic evaluations against human cancer cell lines.
    Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2015, Volume: 28, Issue:5

    The gold(III) complexes of the type (1,2-diaminocyclohexane)(1,3-diaminopropane)gold(III) chloride, [(DACH)Au(pn)]Cl3, [where DACH = cis-, trans-1,2- and S,S-1,2-diaminocyclohexane and pn = 1,3-diaminopropane] have been synthesized and characterized using various spectroscopic and analytical techniques including elemental analysis, UV-Vis and FTIR spectroscopy; solution as well as solid-state NMR measurements. The solid-state (13)C NMR shows that 1,2-diaminocyclohexane (1,2-DACH) and 1,3-diaminopropane (pn) are strongly bound to the gold(III) center via N donor atoms. The stability of the mixed diamine ligand gold(III) was checked by UV-Vis spectroscopy and NMR measurements. The molecular structure of compound 1 (containing cis-1,2-DACH) was determined by X-ray diffraction analysis. The structure of 1 consists of [(cis-DACH)Au(pn)](3+) complex ion and chloride counter ions. Each gold atom in the complex ion adopts a distorted square-planar geometry. The structural details and relative stabilities of the four possible isomers of the complexes were also estimated at the B3LYP/LANL2DZ level of theoretical calculations. The computational study demonstrates that trans- conformations are slightly more stable than the cis- conformations. The antiproliferative effects and cytotoxic properties of the mixed ligand gold(III) complexes were evaluated in vitro on human gastric SGC7901 and prostate PC3 cancer cells using MTT assay. The antiproliferative study of the gold(III) complexes on PC3 and SGC7901 cells indicate that complex 3 (containing 1S,2S-(+)-1,2-(DACH)) is the most effective antiproliferative agent. The IC50 data reveal that the in vitro cytotoxicity of complex 3 against SGC7901 cancer cells manifested similar and very pronounced cytotoxic effects with respect to cisplatin. Moreover, the electrochemical behavior, and the interaction of complex 3 with two well-known model proteins, namely, hen egg white lysozyme and bovine serum albumin is also reported.

    Topics: Animals; Cattle; Cell Line, Tumor; Cell Proliferation; Chickens; Chlorides; Coordination Complexes; Cyclohexylamines; Diamines; Gold; Humans; Magnetic Resonance Spectroscopy; Muramidase; Serum Albumin, Bovine; Ultraviolet Rays; X-Ray Diffraction

2015
Trans-cyclohexanediamines prevent thermal inactivation of protein: role of hydrophobic and electrostatic interactions.
    The protein journal, 2008, Volume: 27, Issue:4

    Although solution additives prevent protein misfolding, the mechanism remains elusive. In this paper, we compare the preventive effects of trans-1,2-cyclohexanediamine (1,2-CHDA) and trans-1,4-cyclohexanediamine (1,4-CHDA) on the heat-induced inactivation of ribonuclease A (RNase A) and lysozyme. These additives are more effective in preventing thermal inactivation of the proteins than guanidine (Gdn) and arginine (Arg). The results suggest two possibilities: (i) decrease in the hydrophobic interaction between unfolded protein molecules is indispensable for preventing protein association, and (ii) the electrostatic interaction between additives interacting with the hydrophobic residues of protein molecules plays an important role in preventing thermal inactivation of proteins.

    Topics: Animals; Cyclohexylamines; Hot Temperature; Hydrophobic and Hydrophilic Interactions; Muramidase; Protein Folding; Ribonuclease, Pancreatic; Static Electricity; Stereoisomerism

2008