01985nas a2200265   4500008004100000022001400041245006200055210006100117260010600178300001000284490000700294520110800301653001401409653001401423653003201437653001601469653001601485653001701501653002001518100002201538700002201560700002201582700002001604856009501624       2015                        eng d  a0965-174800aCathepsins of lepidopteran insects: aspects and prospects0 aCathepsins of lepidopteran insects aspects and prospects  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcSEP  a51-590 v643 a<p>Molecular understanding of lepidopteran physiology has revealed that proteases consist of one of the central regulatory/reacting system for insect growth and survival. Among the various proteases, cathepsins are the most crucial cellular proteases, which play vital roles during insect development. In the present review, we have discussed various aspects of the lepidopteran insect cathepsins, emphasizing their roles in processes like development, growth, metamorphosis, apoptosis and immunity. Cathepsins are categorized into different types on the basis of their sequence diversification, leading to variation in structure and catalytic function. Cathepsins exhibit tissue and stage specific expression pattern which is fine-tuned by a delicate balance of expression, compartmentalization, zymogen activation, inhibition by protein inhibitors and degradation. The indispensability of cathepsins as cellular proteases in the above mentioned processes proposes them as novel targets for designing effective and specific insect controlling strategies. (C) 2015 Elsevier Ltd. All rights reserved.</p>10aApoptosis10aCathepsin10aCysteine/aspartate protease10aDevelopment10aLepidoptera10aPest control10aStress response1 aSaikhedkar, Nidhi1 aSummanwar, Aarohi1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/cathepsins-lepidopteran-insects-aspects-and-prospects-002795nas a2200265   4500008004100000022001400041245014500055210006900200260000800269300001400277490000900291520187200300653001902172653001602191653001702207653002302224653001802247100002702265700002202292700002002314700002002334700002402354700002002378856013102398       2019                        eng d  a0304-416500aPhyto-inspired cyclic peptides derived from plant Pin-II type protease inhibitor reactive center loops for crop protection from insect pests0 aPhytoinspired cyclic peptides derived from plant PinII type prot  cAUG  a1254-12620 v18633 a<p>Background: Natural defence of plants against insect pests involves protease inhibitors (PIs) that interfere with insect digestive proteases. Pin-II type plant PIs are wound inducible upon insect damage and possess multiple inhibitory repeat domains that can inhibit trypsin and chymotrypsin-like proteases in the insect midgut. Yet, their agricultural ex-vivo application is limited due to large molecular size and environmental instability, which could be overcome by small peptides. Methods: Bicyclic peptides were designed by grafting Pin-II PIs derived reactive center loop (RCL) on synthetic tris(bromomethyl)benzene scaffold. In vitro binding with trypsin-like proteases was evaluated by biochemical and biophysical assays, followed by molecular dynamics simulations. In vivo effects on two major lepidopteran insect pests, Helicoverpa armigera and Spodoptera litura were studied upon feeding with peptide treated leaves. Affinity based pull down assays were used to identify target proteins in insect gut. Results: Bicyclic RCLs showed ten-fold enhanced protease inhibition compared to their linear counterparts. They exhibited feeding deterrence and growth reduction of lepidopteran insects. Bicyclic peptides predominantly interact with midgut serine proteases. Possible binding modes involve simultaneous interaction with the active site and specificity-determining residues of insect gut trypsin. Conclusion: Bicyclic peptides are potent inhibitors of serine proteases in the insect midgut. They cause feeding aversion and larval growth retardation. Bi-domain cyclic peptides interact with two sites on trypsin, leading to enhanced efficacy over linear RCL peptides. General significance: Bicyclic peptides mimic natural PIs by inhibiting insect proteases leading to growth reduction, thus, could be used as pest control molecules in agriculture.</p>
10aCyclic peptide10aLepidoptera10aPest control10aprotease inhibitor10aReactive loop1 aSailthedkar, Nidhi, S.1 aJoshi, Rakesh, S.1 aYadav, Amit, K.1 aSeal, Shubhendu1 aFernandes, Moneesha1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/phyto-inspired-cyclic-peptides-derived-plant-pin-ii-type-protease-inhibitor-reactive-center02323nas a2200265   4500008004100000022001400041245013000055210006900185260000800254300001200262490000700274520144300281653001201724653001301736653002401749653001801773653001501791653001201806653001701818100002201835700002601857700002201883700002001905856013201925       2023                        eng d  a1572-388700aDomain shuffling and site-saturation mutagenesis for the enhanced inhibitory potential of amaranthaceae α-amylase inhibitors0 aDomain shuffling and sitesaturation mutagenesis for the enhanced  cOCT  a519-5320 v423 a<p>
	Amaranthaceae a-amylase inhibitors (AAIs) are knottin-type proteins with selective inhibitory potential against coleopteran a-amylases. Their small size and remarkable stability make them exciting molecules for protein engineering to achieve superior selectivity and efficacy. In this report, we have designed a set of AAI pro- and mature peptides chimeras. Based on in silico analysis, stable AAI chimeras having a stronger affinity with target amylases were selected for characterization. In vitro studies validated that chimera of the propeptide from Chenopodium quinoa a-AI and mature peptide from Beta vulgaris a-AI possess 3, 7.6, and 4.26 fold higher inhibition potential than parental counterparts. Importantly, recombinant AAI chimera retained specificity towards target coleopteran a-amylases. In addition, to improve the inhibitory potential of AAI, we performed in silico site-saturation mutagenesis. Computational analysis followed by experimental data showed that substituting Asparagine at the 6th position with Methionine had a remarkable increase in the specific inhibition potential of Amaranthus hypochondriacus a-AI. These results provide structural-functional insights into the vitality of AAI propeptide and a potential hotspot for mutagenesis to enhance the AAI activity. Our investigation will be a toolkit for AAI's optimization and functional differentiation for future biotechnological applications.</p>
10a& alpha10a-Amylase10a-Amylase inhibitors10aAmaranthaceae10aColeoptera10aPeptide10aPest control1 aRane, Ashwini, S.1 aNair, Vineetkumar, S.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/domain-shuffling-and-site-saturation-mutagenesis-enhanced-inhibitory-potential-amaranthaceae