@article {46128,
	title = {NMR structure and dynamics of inhibitory repeat domain variant 12, a plant protease inhibitor from Capsicum annuum, and its structural relationship to other plant protease inhibitors},
	journal = {Journal of Biomolecular Structure \& Dynamics},
	year = {2019},
	month = {APR},
	type = {Article; Early Access},
	abstract = {<p>Although several plant protease inhibitors have been structurally characterized using X-ray crystallography, very few have been studied using NMR techniques. Here, we report an NMR study of the solution structure and dynamics of an inhibitory repeat domain (IRD) variant 12 from the wound-inducible Pin-II type proteinase inhibitor from Capsicum annuum. IRD variant 12 (IRD12) showed strong anti-metabolic activity against the Lepidopteran insect pest, Helicoverpa armigera. The NMR-derived three-dimensional structure of IRD12 reveals a three-stranded anti-parallel beta-sheet rigidly held together by four disulfide bridges and shows structural homology with known IRDs. It is interesting to note that the IRD12 structure containing similar to 75\% unstructured part still shows substantial amount of rigidity of N-H bond vectors with respect to its molecular motion. Communicated by Ramaswamy H. Sarma</p>
},
	keywords = {Bt transgenic, Capsicum annuum, Helicoverpa armigera, inhibitory repeating domains, NMR structure, Protease inhibitors (PIs)},
	issn = {0739-1102},
	doi = {10.1080/07391102.2019.1607559, Early Access Date = APR, Early Access Year = 2019},
	author = {Gartia, Janeka and Anangi, Raveendra and Joshi, Rakesh S. and Giri, Ashok P. and King, Glenn F. and Barnwal, Ravi P. and Chary, Kandala V. R.}
}
@article {49511,
	title = {Novel bifunctional inhibitor of protease and α-amylase from Clitorea ternatea restricts the growth and development in Spodoptera frugiperda},
	journal = {International Journal of Biological Macromolecules},
	volume = {305},
	year = {2025},
	month = {MAY},
	pages = {141180},
	type = {Article},
	abstract = {<p>
	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.</p>
},
	keywords = {alpha-Amylase inhibitors, Bifunctional inhibitor, Clitoria ternatea, Protease inhibitors, Spodoptera frugiperda},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2025.141180},
	author = {Dongare, Pratiksha M. and Madage, Varsha A. and Deshpande, V. Neha and Joshi, Rakesh S. and Giri, Ashok P. and Pawar, Pankaj K.}
}
