3095-79-2Relevant academic research and scientific papers
Relationship between Chemical Selectivity and Melting Points of Reacting Molecules
Endo, Tadashi,Takeda, Yukiko,Orii, Toyohiko,Kuwahara, Akio,Ohara, Masahiro
, p. 2687 - 2688 (1980)
A relationship has been found to exist between the selectivity (the ratio of an unsymmetrical disulfide to symmetrical one) in the oxidation of a pair of associating thiols, 1-acyl-3-(2-sulfydrylethyl)urea (1) and 1-(p-N,N-dimethylaminophenyl)-3-(sulfhydrylacetyl)urea, and the melting point of 1 in cases where 1 belongs to a homologous series.
Synthesis and Biological Evaluation of Dithiobisacetamides as Novel Urease Inhibitors
Liu, Mei-Ling,Li, Wei-Yi,Fang, Hai-Lian,Ye, Ya-Xi,Li, Su-Ya,Song, Wan-Qing,Xiao, Zhu-Ping,Ouyang, Hui,Zhu, Hai-Liang
, (2021/11/13)
Thirty-eight disulfides containing N-arylacetamide were designed and synthesized in an effort to develop novel urease inhibitors. Biological evaluation revealed that some of the synthetic compounds exhibited strong inhibitory potency against both cell-free urease and urease in intact cell with low cytotoxicity to mammalian cells even at concentration up to 250 μM. Of note, 2,2′-dithiobis(N-(2-fluorophenyl)acetamide) (d7), 2,2′-dithiobis(N-(3,5-difluorophenyl)acetamide) (d24), and 2,2′-dithiobis(N-(3-fluorophenyl)acetamide) (d8) were here identified as the most active inhibitors with IC50 of 0.074, 0.44, and 0.81 μM, showing 32- to 355-fold higher potency than the positive control acetohydroxamic acid. These disulfides were confirmed to bind urease without covalent modification of the cysteine residue and to inhibit urease reversibly with a mixed inhibition mechanism. They also showed very good anti-Helicobacter pylori activities with d8 showing a comparable potency to the clinical used drug amoxicillin. The impressive in vitro biological profile indicated their immense potential as therapeutic agents to tackle H. pylori caused infections.
Monolayer assemblies of a de novo designed 4-α-helix bundle carboprotein and its sulfur anchor fragment on Au(111) surfaces addressed by voltammetry and in situ scanning tunneling microscopy
Brask, Jesper,Wackerbarth, Hainer,Jensen, Knud J.,Zhang, Jingdong,Chorkendorff, Ib,Ulstrup, Jens
, p. 94 - 104 (2007/10/03)
Mapping and control of proteins and oligonucleotides on metallic and nonmetallic surfaces are important in many respects. Electrochmical techniques based on single-crystal electrodes and scanning probe microscopies directly in aqueous solution (in situ SPM) have recently opened perspectives for such mapping at a resolution that approaches the single-molecule level. De novo design of model proteins has evolved in parallel and holds promise for testing and controlling protein folding and for new tailored protein structural motifs. In this report we combine these two strategies. We present a scheme for the synthesis of a new 4-α-helix bundle carboprotein built on a galactopyranoside derivative with a thiol anchor aglycon suitable for surface immobilization on gold. The carboprotein with thiol anchor in monomeric and dimeric (disulfide) form, the thiol anchor alone, and a sulfur-free 4-α-helix bundle carboprotein without thiol anchor have been prepared and investigated for comparison. Cyclic and differential pulse voltammetry (DPV) of the proteins show desorption peaks around -750 mV (SCE), whereas the thiol anchor desorption peak is at -685 mV. The peaks are by far the highest for thiol monomeric 4-α-helix bundle carboprotein and the thiol anchor. This pattern is supported by capacitance data. The DPV and capacitance data for the thiolated 4-α-helix bundle carboproteins and the thiol anchor hold a strong Faradaic reductive desorption component as supported by X-ray photoelectron spectroscopy. The desorption peak of the sulfur-free 4-α-helix bundle carboprotein, however, also points to a capacitive component. In situ scanning tunneling microscopy (in situ STM) of the thiol anchor discloses an adlayer with small domains and single molecules ordered in pin-striped supramolecular structures. In situ STM of thiolated 4-α-helix bundle carboprotein monomer shows a dense monolayer in a broad potential range on the positive side of the desorption potential. The coverage decreases close to this potential and single-molecule structures become apparent. The in situ STM contrast is also strengthened, indicative of a new redox-based tunneling mechanism. The data overall suggest that single-molecule mapping of natural and synthetic proteins on well-characterized surfaces by electrochemistry and in situ STM is within reach.
Thin Layer Chromatographic Analysis of Some Mercaptoacetamides
Jain, K. K.,Bateja, S.,Bhandari, C. S.
, p. 47 - 48 (2007/10/02)
Thin layer chromatographic studies of N-aryl substituded-2-mercapto acetamides have been made using different solvent systems.Rf values increases regularly with the increase in dieletric constant of the solvent in the order CHCl3 > CH3COCH3 > (
SIMILARITY IN THE STRUCTURE OF THE BINDING SITES BETWEEN A PAIR OF REACTING MOLECULES: ITS EFFECT OF MOLECULAR RECOGNITION
Endo, Tadashi,Takeda, Yukiko,Kamada, Hiroko,Kayama, Shigeo,Tasai, Hidetoshi
, p. 417 - 420 (2007/10/02)
Based on the selectivity in the oxidation of a pair of thiols (1 and 2) with O2, it is suggested that maximal recognition between 1 and 2 occurs when 1 and 2 are similar in the structure of the binding sites to each other.
SPECIFIC WEAK INTERACTIONS RELATED TO GEOMETRICAL SHAPE OF ASSOCIATING THIOLS: THE FACTOR RESPONSIBLE FOR SELECTIVE MOLECULAR RECOGNITION IN THEIR OXIDATION
Endo, Tadashi,Takeda, Yukiko,Orii, Toyohiko,Murata, Tomoji,Sakai, Miyuki,et al.
, p. 1291 - 1294 (2007/10/02)
In oxidation of a pair of associating thiols (1d and 2) with O2, specific weak interactions related to their geometrical shape such as CH...N and CH...SH interactions are suggested to be responsible for selective molecular recognition.
