Hydrolytic enzyme-peptide interactions

PPEs have recently been utilized in the dosimetric detection of proteases [197,198]. PPE 131 was substituted with an oligopeptide that carries a dinitroaniline quencher. The oligopeptide contains a motif that is susceptible toward protease action. This construct is nonfluorescent, because the dangling dinitroaniline imits quench the PPE s fluorescence. Upon exposure to low loadings of trypsine, a nonselective hydrolytic enzyme, the fluorescence of the quencher-less PPE 132 is observed. The oligopeptide chain was selected because it could be a substrate for matrix metalloproteases (human collagenase III) associated with human cancer cells. The peptide does not have to be covalently attached to the PPE Pinto and Schanze [198] were able to demonstrate that electrostatic interactions are likewise efficient in the detection of proteases by PPEs (Scheme 6.41). 

Formal PK drug-drug interaction studies have not been performed with Prialt. As ziconotide is a peptide, it is expected to be completely degraded by endopeptidases and exopeptidases (Phase I hydrolytic enzymes) widely located throughout the body, and not by other Phase I biotransformation processes (including the cytochrome P450 system) or by Phase... 

Table IV. Interaction Between an Antifungal Peptide and a Hydrolytic Enzyme...

This cyclic interaction profile is considered for other types of myosin that determine the pwasons direction along the actin filament [38-40]. A similar mechanism based on proton-induced water solitons is suggested for ATP hydrolysis by dynein or kinesin along microtubules, or by G-actin polymerization [41], as well as for other substrates of various hydrolytic enzymes. Thus, a hydraulic drive due to AS is proposed to translocate the ATPase machinery of DNA replication, RNA transcription, or peptide translation. These processes can be effectively associated with active flow of substrates and products across the catalytic regions. 

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