Charges' interaction in polyelectrolyte (nano)complexing of His6-OPH with peptides: Unpredictable results due to imperfect or useless concept?

Enzymatically Functionalized Composite Materials Based on Nanocellulose and Poly(Vinyl Alcohol) Cryogel and Possessing Antimicrobial Activity

“…Based on the catalytic data alone, one can conclude that the PVA-CG/BC/His 6 -OPH/indolicidin composite is the best choice (Figure 2). Actually, the enzyme activity was already aligned between the different composites at 24 h, and based on antibacterial activity measurements, there was a strong negative influence of BC (Figure 3) in spite of the significantly improved antibacterial activity of His 6 -OPH/indolicidin [8]. Indolicidin has three positively charged amino acids (arginines and lysine) and can electrostatically interact not only with enzyme but also with BC.…”

“…It has a wide specificity with a number of AHLs in addition to high catalytic activity toward toxic organophosphorus compounds [5,6]. His 6 -OPH in noncovalent complexes with various antimicrobial agents (antibiotic and, particularly, antimicrobial peptides) has been shown to improve the activity of each other [7,8,9]. As a result, the enzyme has a wider substrate spectrum toward different AHLs in such combinations, and its stability is increased [7,8,9].…”

“…In other words, the aim of the study was to form an immobilized biocatalyst possessing good operational characteristics and exhibiting certain antimicrobial and catalytic properties. Yet another task was to evaluate the bactericidal characteristics of similar composites prepared with additives of β-lactam antibiotic or antimicrobial peptides, both forming noncovalent complexes with His 6 -OPH [7,8,9]. The development of such composite biomaterials with bactericidal properties can be considered an important task in view of the rapid increase in the number of antibiotic-resistant pathogenic microorganisms and a significant decrease in the effectiveness of action of the known and commonly used antibiotics.…”

Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions

“…Nevertheless, active variants of ALP and ACP acting on triesters are often isolated from insect pests and plants that have evolved resistance to the pesticides used, including due to these enzymes. As a result of this accelerated evolution (Figures 13 and 14), the resulting variants (being predicted in a similar procedure with [64]) inherit the main structural motif of their precursor proteins (Figure 12a,b). The structure of ALP monomer (A), ACP monomer (B), and CYP1A1 monomer (C) according to data (UniProt A0A2W1BMI5, UniProt Q9MB07, and PDB 4I8V, respectively).…”

“…The entrance to the active centers of the enzymes is framed, and their structures are shown in detail within insets. The structures of ALP and ACP were predicted with I-TASSER server (http://zhanglab.ccmb.med.umich.edu/I-TASSER/) as described in [64]; after that the residues of the active centers were aligned with known structural homologues (PDB 1K7H and 1KBP, respectively), and coordinates of metal ions were determined and used further. The binding of the substrate methyl paraoxon (A,B) and methyl parathion (C) was determined as previously.…”