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... non-competitive inhibition, there is no similarity between the structure of the substrate and the inhibitor. The inhibitors bind with the enzyme at sites other than the substrate binding site leading to the formation of both enzyme-inhibitor (EI) and enzyme-inhibitor-substrate (EIS) complexes. [21] (Fig. 5). The inhibitor forms non-covalent bonding with the enzyme and so the enzyme inhibition can be reversed by simply removing the inhibitor. The catalysis is still stopped; the reason behind this may be distortion in the enzyme conformation [20] ...
Citations
... The proelastase is the inert form of enzyme elastase activation of proelastase is through cleavage of sub-unit residues that bind to the major component of the protein. (Pathak et al., 2020). Structure and action of elastase enzyme show in figure (1-1). ...
... Caspases is one of the important enzymes secreted during various metabolic processes such as apoptosis, necrosis, and inflammation. It plays a major and central role in cells for programmed death during the progressing (Pathak et al., 2020). The caspases exist in its inactive form but it converts to the active form through proteolysis at specific asparagine residues located inside the pro-domain. ...
The study aimed to inhibit the virulence factors in Pseudomonas aeruginosa (activity of elastase enzyme, biofilm formation and growth of bacteria) by construction specific nanocomposite. The nanocomposite (AgPEG-I) was synthesized using the specific enzyme inhibitor galaridin which was chemically coupled to the surface of silver nanoparticles coated with polyethylene glycol (AgPEG) using special coupling agents (EDC/ NHS).
Main steps of research project are summarized as follow
1- Isolation and identification of Pseudomonas aeruginosa from different clinical sample using biochemical test.
2- Selection of the high virulence P. aeruginosa isolate for antibiotic resistance , elastase activity and biofilm formation.
3- Kinetics studying of elastase activity and inhibition by galardin inhibitor (GM6001).
4- Synthesis of nanocomposite AgPEG-I (AgPEG coupling with galardin inhibitors).
5- Characterization of nanocomposite (AgPEG-I) by AFM, SEM, XRD, FTIR and Zeta potential assay.
6- Evaluation of cytotoxicity of nanocomposite (AgPEG-I) by using MTT (cell viability), High-content screening (HCS) to measurement multiple parameters and Flow cytometer assay (cell cycle analysis).
7- Applications the nanocomposite (AgPEG-I) on determination the virulence state through the inhibition of elastase activity, biofilm production and viability of bacterial cells.
