scholarly journals The Potential of RIP (Ribosome Inactivating Protein) as Biopesticides

Buletin Eboni ◽  
2019 ◽  
Vol 1 (1) ◽  
pp. 33-39
Author(s):  
Tati Suharti ◽  
Dharmawati F Djam’an
Keyword(s):  
Protein Synthesis ◽  
Broad Spectrum ◽  
Plant Pathogen ◽  
Mode Of Action ◽  
Castor Bean ◽  
Insect Pests ◽  
Bitter Melon ◽  
Ribosome Inactivating Protein ◽  
High Potency ◽  
Anti Fungal

RIP (Ribosome Inactivating Protein) produced by plants that can act as a plant defense from pest and disease. This protein is widely used as an anti-fungal, anti-bacterial, anti-virus and anti-insect. Therefore, RIP contained in plants has the potential to be used for environmentally friendly biopesticides. The purpose of this paper is to provide information on RIP derived from plants and its potential as a biopesticide.The mode of action of RIP works is by inhibiting protein synthesis during translating process of pest and plant pathogen. RIP has a broad spectrum so that it can overcome insect pests from various orders and pathogens both fungi, bacteria and viruses. Some types of plants that contain RIP include neem, ginger, turmeric, galangal, castor bean, jatropha, soursop and bitter melon. RP applications can be in the form of oil, essential oils, solutions, flour, ash and simplicia. RIP can be applied to seeds, seeds, plants and post-harvest products. The advantages of using RIP include easily available materials, inexpensive, easy to application and environmentally friendly.The plants contain RP has high potency to commercially developed so in the future, the controlling of pest and disease rely on the plants contain RIP both direct and in the pesticides formulations form. Therefore echo friendly plantation programme can be realized.

scholarly journals The acylation of proteins by xenobiotic amphipathic carboxylic acids in cultured rat hepatocytes

1988 ◽  
Vol 254 (1) ◽  
pp. 39-44 ◽  
Author(s):  
R Hertz ◽  
J Bar−Tana
Keyword(s):  
Protein Synthesis ◽  
Carboxylic Acids ◽  
Mode Of Action ◽  
Biological Effects ◽  
Rat Hepatocytes ◽  
Protein Adducts ◽  
Cultured Rat Hepatocytes ◽  
Acylated Proteins ◽  
Dose Dependent ◽  
Protein Acylation

Three xenobiotic amphipathic carboxylates, namely MEDICA 16, nafenopin and bezafibrate, which differ remarkably in their hydrophobic backbones, were found to acylate membrane and cytosolic liver proteins in cultured rat hepatocytes. The acylation patterns observed were time- and dose-dependent, and the acylated residue consisted of the original xenobiotic. The acylation patterns generated by the three xenobiotic carboxylates included common proteins which were acylated by the three xenobiotics (e.g. proteins of 32, 52, 56 and 72 kDa) as well as unique proteins which were specifically acylated by the respective xenobiotics. The acylation of liver proteins by either MEDICA 16 or nafenopin remained unaffected under conditions where protein synthesis was completely inhibited by cycloheximide. Protein acylation thus offers a common mode of action of xenobiotic amphipathic carboxylates, which may, however, result in diverse xenobiotyl-protein adducts. The xenobiotyl-acylated proteins might be involved in triggering some of the biological effects exerted by xenobiotic amphipathic carboxylates employed as hypolipidaemic effectors, peroxisomal proliferators or preadipocyte convertors.

Broad Spectrum and Mode of Action of an Antibiotic Produced by Scytonema sp. TISTR 8208 in a Seaweed-Type Bioreactor

1998 ◽  
pp. 249-256
Author(s):  
Aparat Chetsumon ◽  
Fusako Umeda ◽  
Isamu Maeda ◽  
Kiyohito Yagi ◽  
Tadashi Mizoguchi ◽  
...  
Keyword(s):  
Broad Spectrum ◽  
Mode Of Action

scholarly journals The Search for Antifungals from Amazonian Trees: A Bio-Inspired Screening

2015 ◽  
Vol 10 (4) ◽  
pp. 1934578X1501000
Author(s):  
Charlie Basset ◽  
Véronique Eparvier ◽  
Laila S. Espindola
Keyword(s):  
Antifungal Activity ◽  
Ethyl Acetate ◽  
Broad Spectrum ◽  
Tree Species ◽  
French Guiana ◽  
Antifungal Agents ◽  
Ethyl Acetate Extract ◽  
Natural Durability ◽  
Anti Fungal ◽  
Amazonian Trees

The anti-fungal activity of 60 extracts from 15 tree species in the French Guiana rainforest against human and wood-rotting fungi was studied. In this way (+)-mopanol (1) was isolated from the ethyl acetate extract of Peltogyne sp. (Caesalpiniaceae) wood. This work demonstrated that (1) the natural durability of wood can indeed guide the search for antifungal agents, (2) that extracts selected in this bio-inspired process exhibit a broad spectrum of antifungal activity and (3) that the method allows for the isolation of strongly active antifungals.

OESTROGEN – ANTI-OESTROGEN INTERACTION: EFFECT OF U11100A, MRL-41 (CLOMIPHENE) AND U11555A ON OESTROGEN INDUCED UTERINE GLYCOGEN AND PROTEIN SYNTHESIS IN THE RAT DURING DELAYED IMPLANTATION

1969 ◽  
Vol 62 (3) ◽  
pp. 489-497 ◽  
Author(s):  
Suresh Mohla ◽  
M. R. N. Prasad
Keyword(s):  
Protein Synthesis ◽  
Comparative Study ◽  
Interaction Effect ◽  
Mode Of Action ◽  
Biochemical Changes ◽  
Delayed Implantation ◽  
Receptor Sites ◽  
Made In

ABSTRACT A comparative study of three non-steroidal anti-oestrogens (a dihydronaphthalene, UlllOOA; a diphenylindene derivative, U-11555A and MRL-41 (clomiphene) was made in order to study their mode of action and their interaction with oestrogen induced biochemical changes in the uterus. Pretreatment with UlllOOA, clomiphene or U11555A effectively blocked the oestrogen induced increase in uterine glycogen and protein synthesis. However, all the three compounds tested were found to be uterotrophic; clomiphene also increased uterine glycogen while U11555A showed a transient oestrogenic action in increasing uterine protein. Clomiphene and U11100A have been shown to inhibit the uptake of oestrogen at the receptor sites. Our results may be interpreted as indicating that pretreatment with these compounds (U11100A, clomiphene or U11555A) blocked the uterine receptor sites in such a manner so as to render ineffective the action of oestrogen administered subsequently.

scholarly journals Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms

2020 ◽  
Vol 2 ◽  
Author(s):  
Aurélie H. Benfield ◽  
Sónia Troeira Henriques
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties ◽  
Broad Spectrum ◽  
Mode Of Action ◽  
Bacterial Pathogens ◽  
Model Membranes ◽  
Membrane Disruption ◽  
Attractive Alternative ◽  
Bacterial Cells

Antimicrobial peptides are an attractive alternative to traditional antibiotics, due to their physicochemical properties, activity toward a broad spectrum of bacteria, and mode-of-actions distinct from those used by current antibiotics. In general, antimicrobial peptides kill bacteria by either disrupting their membrane, or by entering inside bacterial cells to interact with intracellular components. Characterization of their mode-of-action is essential to improve their activity, avoid resistance in bacterial pathogens, and accelerate their use as therapeutics. Here we review experimental biophysical tools that can be employed with model membranes and bacterial cells to characterize the mode-of-action of antimicrobial peptides.

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