02543nas a2200205 4500008004100000022001400041245015800055210006900213260007900282300001400361490000700375520170700382653002202089653002002111653002402131653001802155100002102173700001402194856012902208 2009 eng d a0196-978100aDifferential elicitation of an aspartic protease inhibitor: regulation of endogenous protease and initial events in germination in seeds of vigna radiata0 aDifferential elicitation of an aspartic protease inhibitor regul a360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USAbELSEVIER SCIENCE INCcDEC a2118-21260 v303 a

Plant aspartic proteases are of recent origin with their physiological significance in crucial processes emerging. Reports on the significance of aspartic protease inhibitors and their endogenous proteases in seeds of plants are scanty. This paper reports the purification of an aspartic protease inhibitor from the seeds of Vigna radiata, its control of the endogenous aspartic protease and their subsequent role in the early germination events. The role of the aspartic protease inhibitor and the enzyme in initial stages of germination of V. radiata has been tracked by differential timed expression and germination assays. The expression pattern revealed maximum expression of the inhibitor in the dormant seeds while the enzyme was predominant in the germinating seeds. Their expression patterns and interactions indicate their significance in initiation of germination. The expression of other classes of proteases was monitored during germination and a model predicting the events occurring during proteolysis of the storage protein in germination is hypothesized. The inhibitor was a linear, hydrophobic, pH stable and thermostable peptide with molecular weight of 1660 Da. The purified inhibitor showed a pI of 4.36 with the sequence as AEIYN KDGNK LDLYG. The inhibitor was found to be stable in a broad range of pH from 2 to 10 with an optimum of 3.0. The half-life of VrAPI at 100 degrees C was 30 min whereas the maximum activity was observed at 37 degrees C. The initial kinetic analysis of the inhibitor against the enclogenous protease showed an IC50 value of 11 nM while the value of the inhibition rate constant K-i was 34 x 10(-9) M. (C) 2009 Elsevier Inc. All rights reserved.

10aAspartic protease10aPlant proteases10aProtease inhibitors10aVigna radiata1 aKulkarni, Aarohi1 aRao, Mala uhttps://library.ncl.res.in/content/differential-elicitation-aspartic-protease-inhibitor-regulation-endogenous-protease-and-001524nas a2200229 4500008004100000022001400041245012100055210006900176260010600245300001400351490000700365520061200372653001300984653002100997653002401018653001401042653002501056653002701081100002801108700002701136856013101163 2011 eng d a0968-089600aDesign, synthesis and biological evaluation of peptidyl-vinylaminophosphonates as novel cysteine protease inhibitors0 aDesign synthesis and biological evaluation of peptidylvinylamino aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcDEC a7129-71350 v193 a

We report herein, design and synthesis of vinylaminophosphonates, a novel class of compounds as possible cysteine protease inhibitors. The synthesis of vinylaminophosphonates has been accomplished employing Tsuji-Trost reaction as a key step. The synthesized compounds were assayed against papain, a model cysteine protease and some of our synthesized compounds showed IC50 values in the range of 30-54 mu M thereby suggesting that these chemical entities thus could constitute an interesting template for the design of potential novel protease inhibitors. (C) 2011 Elsevier Ltd. All rights reserved.

10aCysteine10aInhibitor design10aProtease inhibitors10asynthesis10aTsuji-Trost reaction10aVinylaminophosphonates1 aBhattacharya, Asish, K.1 aRana, Kalpeshkumar, C. uhttps://library.ncl.res.in/content/design-synthesis-and-biological-evaluation-peptidyl-vinylaminophosphonates-novel-cysteine-002540nas a2200289 4500008004100000022001400041245012800055210006900183260011100252300001200363490000600375520148800381653000601869653000601875653003601881653001201917653002801929653002401957653001901981100002202000700001902022700002102041700002102062700002302083700001702106856012702123 2012 eng d a1573-406400aDesign, synthesis and evaluation of unique 2,4,5-triaryl imidazole derivatives as novel potent aspartic protease inhibitors0 aDesign synthesis and evaluation of unique 245triaryl imidazole d aEXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATESbBENTHAM SCIENCE PUBL LTDcMAY a428-4350 v83 a

The 2,4,5-triaryl imidazole derivatives (API) were designed, screened and characterized kinetically & thermo-dynamically against Pepsin and their activity was also tested on the in silico platform. The docking studies of API with Pepsin show that these are novel and unique inhibitors of Aspartic protease. Drug like properties of these compounds were validated in silico based on Lipinski's rule of Five by calculating ClogP, LogS, H-bond acceptors, H-Bond donors, rotational bonds, PSA, PB and BBB values. The Et/Ki and Et/Km values of API show that they follow the Michaelis-Menten kinetics. The binding of inhibitors with proteases was explained by using Van't Hoff plot and thermodynamic parameters viz. free energy (Delta G), Entropy (Delta S) and Enthalpy (Delta H). The Van't Hoff analysis showed that the value of K-i decreases with increase in temperature and the binding of the inhibitor are entropically driven. API act as new potent aspartic protease inhibitors with K-i, for Pepsin, ranges from 3.7 mu M to 16.7 mu M. Strong hydrophobic groups at C-4 & C-5 position in API favor binding of inhibitors with Pepsin. Experiments also showed that among C-2 aryl substituted imidazole, a 4-substitution on aryl ring is preferred and less polar substituent makes the molecule more active whereas polar substituents at 2-position on C-2 aryl ring makes the molecule less active. The docking studies of API with Pepsin further intensify and validate our results.

10a210a410a5-triaryl imidazole derivatives10adocking10aLipinski's rule of Five10aProtease inhibitors10aThermodynamics1 aKhan, Mohd, Sajid1 aAkhtar, Salman1 aSiddiqui, S., A.1 aSiddiqui, M., S.1 aSrinivasan, K., V.1 aArif, J., M. uhttps://library.ncl.res.in/content/design-synthesis-and-evaluation-unique-245-triaryl-imidazole-derivatives-novel-potent-002475nas a2200253 4500008004100000022001400041245014800055210006900203260010600272300001200378490000700390520147200397653002001869653002501889653001101914653002901925653002401954100002801978700002202006700002102028700002102049700002002070856013102090 2014 eng d a0965-174800aIdentification and expression profiling of helicoverpa armigera microRNAs and their possible role in the regulation of digestive protease genes0 aIdentification and expression profiling of helicoverpa armigera  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcNOV a129-1370 v543 a

The present investigation is an effort to determine the possible roles of microRNAs (miRNAs) in the regulation of protease gene expression in Helicoverpa armigera upon exposure to plant protease inhibitors (PIs). Using Illumina platform, deep sequencing of 12 small RNA libraries was performed from H. armigera larvae fed on artificial diet (AD) or recombinant Capsicum annuum PI-7 (rCanPI-7) incorporated diet, at various time intervals (0.5, 2, 6, 12, 24, and 48 h). Sequencing data were analyzed with miRDeep2 software; a total of 186 unique miRNAs were identified from all the 12 libraries, out of which 96 were conserved while 90 were novel. These miRNAs showed all the conserved characteristics of insect miRNAs. Homology analysis revealed that most of the identified miRNAs were insect-specific, and more than 50 miRNAs were Lepidoptera-specific. Several candidate miRNAs (conserved and novel) were differentially expressed in rCanPI-7 fed larvae as compared to the larvae fed on AD. H. armigera miRNAs were found to have target sites in several protease genes as well as in protease regulation related genes such as serine PI and immune reactive PI. As expected, negative correlation in the relative abundance miRNAs and their target mRNAs was evident from qualitative real time polymerase chain reaction analysis. The investigation revealed potential roles of miRNAs in H. armigera protease gene regulation. (C) 2014 Elsevier Ltd. All rights reserved.

10aDeep sequencing10aHelicoverpa armigera10amiRNAs10aProtease gene regulation10aProtease inhibitors1 aLomate, Purushottam, R.1 aMahajan, Neha, S.1 aKale, Sandip, M.1 aGupta, Vidya, S.1 aGiri, Ashok, P. uhttps://library.ncl.res.in/content/identification-and-expression-profiling-helicoverpa-armigera-micrornas-and-their-possible-002356nas a2200265 4500008004100000022001400041245014500055210007000200260000800270300001100278490000800289520139600297653002901693653002701722653002201749653002401771653002601795100002701821700002301848700002001871700002201891700002001913700002201933856013501955 2025 eng d a0141-813000aNovel bifunctional inhibitor of protease and α-amylase from Clitorea ternatea restricts the growth and development in Spodoptera frugiperda0 aNovel bifunctional inhibitor of protease and αamylase from Clito cMAY a1411800 v3053 a

An inhibitor molecule capable of inhibiting a wide range of digestive enzymes without affecting endogenous enzymes is always desirable. We report characterization of CteTAI (M.W. 14 kDa), a bifunctional inhibitor (BFI) protein from the seeds of Clitoria ternatea capable of inhibiting trypsin and alpha-amylase. It retains trypsin inhibition activity up to 60 degrees C and alpha-amylase inhibition up to 40 degrees C. Trypsin inhibition is stable across pH 1-12, while alpha-amylase inhibition is stable between pH 3-7. CteTAI is a noncompetitive inhibitor of trypsin and an uncompetitive inhibitor of alpha-amylase. It selectively inhibits proteases and alpha-amylases from various sources, without affecting alpha-amylase from human saliva and Bacillus spp. Proteomic analysis identified CteTAI as a bifunctional inhibitor exhibiting 41 % similarity to a bifunctional inhibitor from Sesbania bispinosa. Feeding Spodoptera frugiperda larvae with CteTAI-infused diet impaired energy metabolism, resulting in undernourished larvae and malformed adults incapable of flight and mating. Key nutritional indices (RGR, RCR, %ECI, %FDI) were severely reduced, indicating that CteTAI disrupts growth and development by inhibiting multiple protease and alpha-amylase isoforms. Biochemical characterization of newly identified CteTAI suggests its potential application in crop protection.

10aalpha-Amylase inhibitors10aBifunctional inhibitor10aClitoria ternatea10aProtease inhibitors10aSpodoptera frugiperda1 aDongare, Pratiksha, M.1 aMadage, Varsha, A.1 aDeshpande, Neha1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aPawar, Pankaj, K. uhttps://library.ncl.res.in/content/novel-bifunctional-inhibitor-protease-and-%CE%B1-amylase-clitorea-ternatea-restricts-growth-and