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1980, Biochemical and Biophysical Research Communications
Plant protease inhibitors (PPIs) are compounds which play a potent defensive role against pest and pathogens, thereby protecting the plants. In this work we tested different plant extracts to identify extracts containing inhibitor against trypsin activity. Plant extracts were made by homogenizing soaked leaves/seeds/root modification of plants in bicarbonate buffer, pH 9.0.The homogenates were centrifuged at 10,000 rpm at 4°C for 10 minutes. The supernatant containing the soluble proteins were used for protease inhibition assay. Protease inhibition assay was carried out in a total volume of 1 ml containing 67 µl trypsin (Bovine), 25 µl plant extract, 511 µl Tris buffer, 67µl NaCl and 330 µg Nα-Benzoyl-DL-Arginine-P-Nitro Anilide (BAPNA) as substrate. On screening 19 extracts from different plants, we found 9 of them inhibited trypsin activity greater than 40%. The percentage inhibition of these plants are Garcinia xanthochymus (96.7± 0.4 %), Datura stramonium (86.1±1.6%), Ricinus communis (74.05±0.45%), Phyllanthus amarus (72.05±2.15%), Santalum album (64.4±1.7 %), Plectranthus ambonicus (62.15±2.45% ), Croton hirtus ( 55.85±0.9% ), Zea mays (48±2.1% ) and Prunus cerasifera (45.38±0.125%). Of these, to our knowledge no trypsin inhibitor was reported from Garcinia xanthochymus, Datura stramonium, Plectranthus ambonicus, Prunus cerasifera, Phyllanthus amarus, Santalum album, and Croton hirtus. As trypsin is a serine protease, a predominant class of protease in the gut of lepidopteran larvae, this screening will be useful to identify extract containing protease inhibitor against the gut protease of lepidopteran pests. Protease inhibitors from these extracts can be exploited for control of lepidopteran pests. Keywords: trypsin, proteases, plant protease inhibitors, Garcinia xanthochymus, Datura stramonium
Asian Pacific Journal of Tropical Biomedicine
Gene set enrichment analysis of alpha-glucosidase inhibitors from Ficus benghalensis2019 •
Objective: To identify alpha-glucosidase inhibitors from Ficus benghalensis and analyze gene set enrichment of regulated protein molecules. Methods: The phytoconstituents of Ficus benghalensis were queried for inhibitors of alphaglucosidase, also identified as aldose reductase inhibitors. Druglikeness score, absorption, distribution, metabolism, excretion and toxicity profile, biological spectrum, and gene expression were predicated for each compound. Docking study was performed to predict the binding affinity with alpha-glucosidase and aldose reductase and compared with clinically proven molecules. Kyoto Encyclopedia of Genes and Genomes pathway analysis was performed for the regulated genes to identify the modulated pathways. Results: Apigenin, 3,4',5,7-tetrahydroxy-3'-methoxyflavone, and kaempferol were identified as inhibitors of alpha-glucosidase and aldose reductase. Kaempferol was predicted to possess the highest binding affinity with both targets. The p53 signaling pathway was predicted to modulate the majority of protein molecules in diabetes mellitus. All the alpha-glucosidase inhibitors were also predicted as membrane integrity agonist and anti-mutagenic compounds. Conclusions: The current study indicates alpha-glucosidase inhibitors from Ficus benghalensis can act as aldose reductase inhibitors after absorption from the intestinal tract. Furthermore, these phytoconstituents are involved in the regulation of numerous protein molecules and pathways. Hence, the anti-diabetic efficacies of these compounds are due to their action on multiple protein molecules and synergistic effects which should be confirmed by future investigations.
The Journal of Plant Science Research
Review on Plant Protease Inhibitors as Therapeutic Molecules2022 •
Plants contain several phytochemical compounds with capacity to exert therapeutic effects on human beings. One such group of molecules are the Protease inhibitors (PIs) which exert inhibitory activity towards several classes of mammalian, bovine, insect or microbial proteinases/proteases. PIs are polypeptides or proteins capable of forming reversible stoichiometric protein-protein complexes with specific proteolytic enzymes. This inhibits the catalytic function of proteolytic enzymes. Study of PIs is important to control proteolysis as it is the key to control the onset of several disease associated phenomena. Although initially, PIs were considered only as protein degrading enzymes, recent studies point them to be signalling molecules in biological activities. In this article, various classes of plant protease inhibitors and their general mode of actions are discussed. The families belonging to the serine protease class of inhibitors (Serpins) are discussed in detail as these constitute an important class of therapeutically important molecules. Data available on the use of PIs for treating a wide range of human diseases and disorders including the still incurable cancers is reviewed. Literature review confirms wide and successful use of Proteasome inhibitors (with similar activities to PIs) in treatment of haematological malignancies. Synthetic proteasome inhibitors are employed to inhibit the proteasome cascades and thus control disease onset and proliferation. Sharing the similar biological activities with the proteasome inhibitors, gives potential for the plant-based PIs to be experimented for similar uses. An attempt is made to report PIs from several plant species and their ongoing clinical trials to study their therapeutic actions.
Trends in Biotechnology Research
IN VITRO SCREENING OF PROTEINASE INHIBITORS (TRYPSIN, CHYMOTRYPSIN AND HELICOVERPA GUT PROTEINASE INHIBITORS) IN DIFFERENT PLANT TISSUE EXTRACTS2012 •
Most of the plant protection strategies are focused on selection and application of the natural proteinase inhibitors (PIs) against insect pests. In addition, PIs also play a vital role in medicine for treatment of immunity related diseases. PI activity exists mainly in seeds, leaves and flowers of plants. In search of novel PIs, 135 different plant tissue extracts (leaf, flower and seed) were screened for their PI (trypsin, chymotrypsin and Helicoverpa gut proteinase inhibitors) activities by using dot-blot assays. Most of the plant tissues screened revealed moderate PI activity, few showed low PI activity and very few of them showed strong PI activity against trypsin, chymotrypsin and Helicoverpa gut proteinases. The inhibitory potency of positive samples was further determined by solution assays. Five plants namely Arachis hypogaea, Vigna sinensis, Dolichos lablab, Phaseolus aureus and Cassia siamea showed higher activity which ranged from 22.91 to 58.33 %. Higher activities recorded in the seed as compare to leaf and flower tissues. Dolichos lablab showed highest PI activity (58.33 %) followed by Cassia siamea (52.08 %). PI activity was found to be distributed unequally in ammonium sulfate (NH2SO4) fractions.
Aspartic acid proteases participate in many physiological processes and their activities are associated with the spreading of diseases such as Alzheimer's disease, hypertension, cancers, and inflammatory, cardiovascular, viral, and other parasitic diseases. Aspartic proteases have become a widely spoken topic due to human immunodeficiency virus protease and malaria parasite protease that are targeted as key therapeutic intervention points in treating AIDS and malaria, respectively. But, relatively few studies have been reported on natural aspartic inhibitors. Therefore inhibition of proteases is one of the most promising approaches as therapeutic drugs for such conditions. In this case, plants have become a good source of proteinaceous and non-proteinaceous inhibitors. The present study is aimed at the identification, characterization, and partial purification of potent aspartic protease inhibitor/s from several medicinal plants in Sri Lanka. For this study plant samples were collected from Kandy district, Sri Lanka. Aqueous extracts of equal concentrations were prepared separately using fresh mature bark samples from Annona muricata, Garcinia quaesita Pierre, Bauhinia tomentosa, Caesalpinia bonduc, Crotalaria laburnifoloria, Crotalaria micans, Entada zeylanica (kosterm), Erythrina suberosa, Azadirachta indica, and Limonia acidissima L. To our knowledge to recent, there are no aspartate inhibitors identified from these plants. Aspartate inhibitory activity was determined by spectrophotometric stop rate determination method using 0.1mg ml-1 pepsin enzyme, 2.5% bovine hemoglobin substrate with plant extracts (inhibitors). The reaction was terminated by adding 5% TCA solution. The absorbance of the acid-soluble peptides was measured at 280 nm. The inhibitor was purified by ammonium sulfate precipitation and ion exchange chromatography methods. Molecular weight was estimated by dialysis. All the experiments were conducted in duplicate three times. Maximum inhibition of pepsin was shown by Garcinia quaesita Pierre while other species didn't show any significant inhibition of pepsin. Hence for further studies, Garcinia quaesita bark extract was selected. The thermal stability of the inhibitor in the crude extract was studied by incubating the extract at different temperatures and determining the remaining activity. The inhibitors were subjected to ammonium Sulphate precipitation and Ion exchange chromatography, in an attempt to purify the inhibitor/s. Molecular weight was estimated by dialysis which implies that the inhibitors comprise small and large molecules with different molecular weights ranging from less than 3.5 kDa to more than 12 kDa. Crude extract of Garcinia quaesita retained more than 50% of inhibitory activity over a wide range of temperatures (4-95 o C) for 30 minutes and also at 4 o C for one month. But the remaining inhibitory activities of the crude extract incubated at room temperature and 37 o C for one month were 20% and 10%, respectively. This suggests that inhibitor molecules are moderately thermostable. This assay procedure provided a quantitative measurement of the inhibitory activity of the inhibitor/s present in the crude bark extract. Fractions obtained from ammonium sulfate precipitation and ion exchange chromatography didn't show inhibition towards pepsin suggesting that inhibitors could be non-proteinaceous. Further studies on purified inhibitors and necessary to characterize and elucidate the structure of the inhibitors
Anais da Academia Brasileira de Ciências
Action of plant proteinase inhibitors on enzymes of physiopathological importance2009 •
Obtained from leguminous seeds, various plant proteins inhibit animal proteinases, including human, and can be considered for the development of compounds with biological activity. Inhibitors from the Bowman-Birk and plant Kunitz-type family have been characterized by proteinase specificity, primary structure and reactive site. Our group mostly studies the genus Bauhinia, mainly the species bauhinioides, rufa, ungulata and variegata. In some species, more than one inhibitor was characterized, exhibiting different properties. Although proteins from this group share high structural similarity, they present differences in proteinase inhibition, explored in studies using diverse biological models.
Plant Proteinaceous Inhibitors of Proteinases and Alpha Amylases En Oxford Surveys of Plant Molecular and Cell Biology Pag 275 334 Oxford University Press 1987
Plant proteinaceous inhibitors of proteinases and alpha-amylases1987 •
Academia Biology
Flower morphology of selected species of genera Kalanchoe and Bryophyllum in Nigeria2023 •
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