23361-28-6Relevant articles and documents
Inhibition of urease enzyme activity by urea and thiourea derivatives of dipeptides conjugated 2, 3-dichlorophenyl piperazine
Suyoga Vardhan,Kumara,Pavan Kumar,Channe Gowda
, p. 92 - 99 (2017)
Objective: Studies on enzyme inhibition remain an important area of pharmaceutical research since these studies have led to the discoveries of drugs used in a variety of physiological conditions. In search of novel urease enzyme inhibitors, four dipeptide
Structure-activity analysis of peptidic Chlamydia HtrA inhibitors
Agbowuro, Ayodeji A.,Hwang, Jimin,Peel, Emma,Mazraani, Rami,Springwald, Alexandra,Marsh, James W.,McCaughey, Laura,Gamble, Allan B.,Huston, Wilhelmina M.,Tyndall, Joel D.A.
, p. 4185 - 4199 (2019/08/07)
Chlamydia trachomatis high temperature requirement A (CtHtrA) is a serine protease that performs proteolytic and chaperone functions in pathogenic Chlamydiae; and is seen as a prospective drug target. This study details the strategies employed in optimizi
Stereochemical basis for the anti-chlamydial activity of the phosphonate protease inhibitor JO146
Agbowuro, Ayodeji A.,Mazraani, Rami,McCaughey, Laura C.,Huston, Wilhelmina M.,Gamble, Allan B.,Tyndall, Joel D.A.
, p. 1184 - 1190 (2017/10/25)
JO146, a mixture of two diastereomers of a peptidic phosphonate inhibitor for Chlamydial HtrA (CtHtrA), has reported activity against Chlamydia species in both human and koala. In this study we isolated the individual diastereomers JO146-D1 and JO146-D2 (
Synthesis, characterization and in vitro DNA binding and cleavage studies of Cu(II)/Zn(II) dipeptide complexes
Arjmand, Farukh,Jamsheera,Mohapatra
, p. 75 - 85 (2013/08/25)
Novel dipeptide complexes Cu(II)?Val-Pro (1), Zn(II)?Val-Pro (2), Cu(II)?Ala-Pro (3) and Zn(II)?Ala-Pro (4) were synthesized and thoroughly characterized using different spectroscopic techniques including elemental analyses, IR, NMR, ESI-MS and molar conductance measurements. The solution stability study carried out by UV-vis absorption titration over a broad range of pH proved the stability of the complexes in solution. In vitro DNA binding studies of complexes 1-4 carried out employing absorption, fluorescence, circular dichroism and viscometric studies revealed the binding of complexes to DNA via groove binding. UV-vis titrations of 1-4 with mononucleotides of interest viz., 5′-GMP and 5′-TMP were also carried out. The DNA cleavage activity of the complexes 1 and 2 were ascertained by gel electrophoresis assay which revealed that the complexes are good DNA cleavage agents and the cleavage mechanism involved a hydrolytic pathway. Furthermore, in vitro antitumor activity of complex 1 was screened against human cancer cell lines of different histological origin.
NOVEL DIPEPTIDYL PEPTIDASE (DP-IV) COMPOUNDS
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Page/Page column 8, (2010/04/06)
The present invention is directed to novel compounds of formula I and pharmaceutically acceptable salts, enantiomers thereof having inhibiting properties of dipeptidyl peptidase IV enzyme (DP-IV inhibitors). The invention is also directed to pharmaceutical compositions comprising these compounds and the use of these compounds along with its composition in the prevention or treatment of diseases associated with DP-IV enzyme. wherein, A is defined as R3-R4 wherein R3 and R4 are together or independently defined as peptides having amino acids ranging from 1 to 10, B is chemical bond between peptide and substituted amine, R1, and R2 are as defined in specification,
Synthesis and antimicrobial activity of 7-Amino cephalosporanic acid derivatives of amino acids and peptides
Himaja,Desai, Siddharth,Sambanthan, A. Thirugnana,Ranjitha
scheme or table, p. 2914 - 2918 (2010/11/05)
A novel series of 7-amino cephalosporanic acid derivatives of amino acid and peptides were synthesized by solution phase technique. The synthesized compounds were tested for their biological activities against bacterial and fungal organisms. All the compounds showed potent antifungal activity and most of the compounds have shown moderate antibacterial activities. The structures of the newly synthesized compounds were confirmed by IR, 1H NMR and mass spectral analysis.
Novel C2-C3′ N-peptide linked macrocyclic taxoids. Part 2: Synthesis and biological activities of docetaxel analogues with a peptide side chain at C2 and their macrocyclic derivatives
Larroque, Anne-Laure,Dubois, Joelle,Thoret, Sylviane,Aubert, Genevieve,Chiaroni, Angele,Gueritte, Francoise,Guenard, Daniel
, p. 563 - 574 (2008/03/12)
The synthesis of a series of novel docetaxel analogues possessing a peptide side chain at the C2 position as well as peptide macrocyclic taxoids is described. These compounds were designed to mimic a region of the α-tubulin loop equivalent to the paclitax
N-bromosuccinimide oxidation of dipeptides and their amino acids: Synthesis, kinetics and mechanistic studies
Linge Gowda,Kumara,Channe Gowda,Rangappa
, p. 376 - 385 (2008/02/08)
Dipeptides (DP), namely valyl-glycine (Val-Gly), alanyl-proline (Ala-Pro), and valyl-proline (Val-Pro) were synthesized by classical solution phase methods and characterized. The kinetics of oxidation of amino acids (AA) and DP by N-bromosuccinimide (NBS) was studied in the presence of perchlorate ions in acidic medium at 28°C. The reaction was followed spectrophotometrically at λmax = 240 nm. The reactions follow identical kinetics, being first order each in [NBS], [AA], and [DP]. No effect on [H+], reduction product [succinimide], and ionic strength was observed. Effects of varying dielectric constant of the medium and addition of anions such as chloride and perchlorate were studied. Activation parameters have been computed. The oxidation products of the reaction were isolated and characterized. The proposed mechanism is consistent with the experimental results. An apparent correlation was noted between the rate of oxidation of AA and DP.
Inhibitors of tripeptidyl peptidase II. 3. Derivation of butabindide by successive structure optimizations leading to a potential general approach to designing exopeptidase inhibitors
Ganellin, C. Robin,Bishop, Paul B.,Bambal, Ramesh B.,Chan, Suzanne M. T.,Leblond, Bertrand,Moore, Andrew N. J.,Zhao, Lihua,Bourgeat, Pierre,Rose, Christiane,Vargas, Froylan,Schwartz, Jean-Charles
, p. 7333 - 7342 (2007/10/03)
The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase that has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO
Structure-based design, synthesis and biochemical testing of novel and potent Smac peptido-mimetics
Sun, Haiying,Nikolovska-Coleska, Zaneta,Chen, Jianyong,Yang, Chao-Yie,Tomita, York,Pan, Hongguang,Yoshioka, Yoshiko,Krajewski, Krzysztof,Roller, Peter P.,Wang, Shaomeng
, p. 793 - 797 (2007/10/03)
Structure-based design, chemical synthesis and biochemical testing of a series of novel Smac peptido-mimetics as inhibitors of XIAP protein are described. The most potent compound, 6j, has a binding affinity (Ki value) of 24 nM to XIAP BIR3 pro