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Recent Advancements in the Pharmacotherapeutic Perspectives of Some Chalcone Scaffold Containing Natural Compounds as Potential Anti-Virals
Published in Debarshi Kar Mahapatra, Cristóbal Noé Aguilar, A. K. Haghi, Natural Products Pharmacology and Phytochemicals for Health Care, 2021
Debarshi Kar Mahapatra, Sanjay Kumar Bharti, Vivek Asati
HIV protease is an enzyme of proteolytic nature that plays an imperative role in the formation of structural proteins and enzymes. This homodimer essentially breaks the huge viral protein components that have numerous functions in substrate binding, terminal replication steps, cellular progeny maturation, etc. There are two types of proteases that play functional dominance in the biochemical process. The first class of protease enzymes employs an activated water molecule to attack the amide bond carbonyl of the substrate’s scissile bond. In the second class of proteases, a nucleophilic atom of an amino acid side chain is employed to commence amide hydrolysis. Chalcones have been seen to reversibly bind with the protease active site and prevent the proteolytic cleavage steps that metamorphosize the inactive virus components into their fully mature infectious forms. Treatment with protease inhibitors has resulted in 1000 times decrease in plasma HIV levels within 3 months duration [21].
Health effects and the baby boomers — middle age
Published in J. Mangano Joseph, Low-Level Radiation and Immune System Damage, 2018
New AIDS cases rose steadily from 1981 to 1992 (Figure 8.1). Trends after about 1991 are somewhat skewed because of the revised AIDS definition introduced in 1993; but experts generally believe the number of newly diagnosed AIDS cases has leveled off at just under 60,000 a year. Beginning in 1996, the use of new combinations of drugs, featuring those from the protease inhibitor class, offered the potential for slowing the spread of HIV in the body. However, these new drugs are not yet considered an AIDS elixir. Some patients show no benefits, some cannot tolerate the drugs, and long-term effects are not yet proven. Moreover, the medications are extremely expensive and unaffordable to many HIV-positive persons.
An Overview of Protease Inhibitors
Published in Se-Kwon Kim, Marine Biochemistry, 2023
Veena Sreedharan, K.V. Bhaskara Rao
Plants are the source of most naturally occurring protease inhibitors. Molecularly, they are clearly defined as serine protease inhibitors and most of them fall into that category. Thus, we can see that animals, microbes, and plants are not providing inhibitors with the same clarity of understanding as plants (Richardson, 1991). PIs from microorganisms, on the other hand, are small-molecular-weight biomolecules, as opposed to those from plants and animals. Usually found in microbes’ culture filtrate, these molecules are produced when macromolecules are hydrolyzed (Umezawa, 1967). Since Umezawa’s (1982) pioneering work, microorganisms have been used to produce protease inhibitors. Microbiology experts can easily prepare the organisms, extract them, and modify them. Microbial proteolytic enzyme inhibitors are molecule peptides that play virtually no role in microorganisms. The creation of a greater part of these effectual extracellular PIs is credited to actinobacteria, specifically, Streptomyces sp., enlarging to the exhibition of a many optional metabolites under use. They end up being biotechnologically the most assorted and effective metabolite makers among the prokaryotes, creating a lavish amount of antitoxins and making them the main antitoxin producers (Jensen et al., 2005). Although actinobacteria are generally subject to compounds like protease β glucosidase, amylase, cellullase, chitinase, and keratinase for nutraceuticals and in addition, they are an expected wellspring of chemical inhibitors (Manivasagan et al., 2014). It is astonishing to see that more than 10,000 of items were gotten from the 140 recorded genera of actinobacteria (Raja and Prabakarana, 2011). Hence, actinobacteria are been progressively investigated for novel mixtures, the emphasis being on marine actinomycetes recently. Marine climate has been known to create a colossal variety of mixtures. Notwithstanding the variety, the way that investigation of marine climate is as yet in the early stage adds to the significance of abuse of marine creatures.
Protective effect of a protease inhibitor from Agaricus bisporus on Saccharomyces cerevisiae cells against oxidative stress
Published in Preparative Biochemistry and Biotechnology, 2019
Reena Vishvakarma, Abha Mishra
Protease inhibitors are ubiquitous molecules, present in all life forms thus can be obtained naturally from varied sources such as bacteria, cyanobacteria, fungi, plants, insects, and animals. These catalytically control the proteolytic enzymes functioning from cellular to organism level. The protease inhibitors include mostly proteins or peptides, polysaccharides, polyphenols, triterpenes, glycerolipids, and some low-molecular-weight non-proteinaceous compounds.[13,14] They are significant in intracellular metabolism and defense system organization of the host organism. The use of protease inhibitors in therapeutics is evident in cancer, muscular dystrophy, inflammation, rheumatic arthritis, diabetics, disseminated sclerosis, and other diseases.[15] In fungi, one of the most common edible mushrooms Agaricus bisporus (white button mushroom) has been known to possess potential therapeutic properties and has shown effectiveness against high blood glucose and cholesterol levels.[16] A serine protease inhibitor has been obtained from Agaricus bisporus through solid-state fermentation.[17] An attempt has been made to study its effect on the oxidative stress induced by hydrogen peroxide on Saccharomyces cerevisiae yeast cells.