02207nas a2200241 4500008004100000022001400041245008000055210006900135260010600204300001200310490000700322520133200329653000901661653003201670653001901702653001801721653001501739100002501754700002401779700002501803700002601828856011101854 2009 eng d a0731-708500aLC-UV and LC-MS evaluation of stress degradation behaviour of tenatoprazole0 aLCUV and LCMS evaluation of stress degradation behaviour of tena aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcDEC a787-7930 v503 a

In the present study, comprehensive stress testing of tenatoprazole was carried out according to ICH guideline Q1A (R2). Tenatoprazole was subjected to stress conditions of hydrolysis, oxidation, photolysis and neutral decomposition. Additionally, the solid drug was subjected to 50 degrees C for 60 days in dry-bath, and to the combined effect of temperature and humidity at 40 degrees C/75% RH. Extensive degradation was found to occur in acidic, neutral and oxidative conditions. Mild degradation was observed in basic conditions. The drug is relatively stable in the solid-state. The products formed under different stress conditions were investigated by LC and LC-MS. Successful separation of drug from degradation products formed under stress conditions was achieved on a Chemito ODS-3 column [C(18) (5 mu m, 250 mm x 4.6 mm, i.d.)] using methanol: 0.01 M acetate buffer pH 4.5 adjusted with glacial acetic acid (55:45) as the mobile phase at flow rate of 1 mL/min and the peak was detected using a UV detector set at 306 nm. The LC-MS m/z values and fragmentation patterns of degradation products formed under different stress conditions were studied and characterized through LC-MS fragmentation. Based on the results, degradation pathway for drug has been proposed. (C) 2009 Elsevier B.V. All rights reserved.

10aHPLC10aStability-indicating method10aStress studies10aTenatoprazole10aValidation1 aMahadik, Mahadeo, V.1 aBhusari, Vidhya, K.1 aKulkarni, Mahesh, J.1 aDhaneshwar, Sunil, R. uhttps://library.ncl.res.in/content/lc-uv-and-lc-ms-evaluation-stress-degradation-behaviour-tenatoprazole-002403nas a2200313 4500008004100000022001400041245010700055210006900162260007100231300001400302490000700316520127100323653004301594653001201637653001201649653003601661100002501697700002301722700002101745700002901766700002401795700002301819700002201842700002001864700002701884700002601911700002501937856012701962 2012 eng d a1535-389300aLow plasma albumin levels are associated with increased plasma protein glycation and HbA1c in diabetes0 aLow plasma albumin levels are associated with increased plasma p a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcFEB a1391-13960 v113 a

Albumin is one of the most abundant plasma proteins and is heavily glycated in diabetes. In this study, we have addressed whether variation in the albumin levels influence glycation of plasma proteins and HbA1c. The study was performed in three systems: (1) streptozotocin (STZ)-induced diabetic mice plasma, (2) diabetic clinical plasma, and (3) in vitro glycated plasma. Diabetic mice and clinical plasma samples were categorized as diabetic high albumin plasma (DHAP) and diabetic low albumin plasma (DLAP) on the basis of their albumin levels. For the in vitro experiment, two albumin levels, high albumin plasma (HAP) and low albumin plasma (LAP), were created by differential depletion of plasma albumin. Protein glycation was studied by using a combination of two-dimensional electrophoresis (2DE), Western blotting, and LC-MSE. In both mice and clinical experiments, an increased plasma protein glycation was observed in DLAP than in DHAP. Additionally, plasma albumin levels were negatively correlated with HbA1c. The in vitro experiment with differential depletion of albumin mechanistically showed that the low albumin levels are associated with increased plasma protein glycation and that albumin competes for glycation with other plasma proteins.

10aadvanced glycation end products (AGEs)10aAlbumin10aglucose10apost translational modification1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aKote, Sachin, S.1 aGolegaonkar, Sandeep, B.1 aChougale, Ashok, D.1 aShaik, Mahemud, L.1 aDhande, Nitin, L.1 aGiri, Ashok, P.1 aShelgikar, Kishore, M.1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J. uhttps://library.ncl.res.in/content/low-plasma-albumin-levels-are-associated-increased-plasma-protein-glycation-and-hba1c-002639nas a2200265 4500008004100000022001400041245006800055210006800123260000800191300001300199490000700212520181400219100002002033700001802053700002102071700001702092700002102109700002002130700001902150700002902169700002502198700001802223700003202241856010002273 2018 eng d a1369-378600aLimonene inhibits Candida albicans growth by inducing apoptosis0 aLimonene inhibits Candida albicans growth by inducing apoptosis cJUL a 565-5780 v563 a

Anti-Candida potential of limonene was evaluated against planktonic growth, biofilm (adhesion, development and maturation) and morphogenesis of Candida albicans in this study. Limonene is a major constituent of citrus oil and most frequently used terpene in food and beverage industry due to its pleasant fragrance, nontoxic, and is generally recognized as safe (GRAS) flavoring agent as well as treatment option in many gastrointestinal diseases. Limonene exhibited excellent anti-Candida activity and was equally effective against planktonic growth of C. albicans isolates differentially susceptible to FLC (N = 35). Limonene inhibited morphogenesis significantly at low concentration. However, it showed stage dependent activity against biofilm formation, that is, it was more effective against adhesion followed by development and maturation. Limonene also exhibited excellent synergy with FLC against planktonic and biofilm growth. SWATH-MS analysis led to identification of limonene responsive proteins that provided molecular insight of its anti-Candida activity. Proteomic analysis revealed upregulation of proteins involved in cell wall glucan synthesis (Kre6); oxidative stress (Rhr2, Adh7 and Ebp1); DNA damage stress (Mbf1 and Npl3); nucleolar stress (Rpl11, Rpl7, Rpl29, Rpl15) and down regulation of cytoskeleton organization (Crn1, Pin3, Cct8, Rbl2), and so forth, in response to limonene. Limonene mediated down regulation of Tps3 indicates activation of caspase (CaMca1) and induction of apoptosis in C. albicans. These results suggest that limonene inhibits C. albicans growth by cell wall/membrane damage induced oxidative stress that leads to DNA damage resulting into modulation of cell cycle and induction of apoptosis through nucleolar stress and metacaspase dependent pathway.

1 aThakre, Archana1 aZore, Gajanan1 aKodgire, Santosh1 aKazi, Rubina1 aMulange, Shradha1 aPatil, Rajendra1 aShelar, Amruta1 aSanthakumari, Bayitigeri1 aKulkarni, Mahesh, J.1 aKharat, Kiran1 aKaruppayil, Sankunny, Mohan uhttps://library.ncl.res.in/content/limonene-inhibits-candida-albicans-growth-inducing-apoptosis