Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli.

Alkyl hydroperoxide reductase subunit C from Pseudomonas aeruginosa PAO1 (PaAhpC) is a member of the 2-Cys peroxiredoxin family. Here, we examined the peroxidase and molecular chaperone functions of PaAhpC using a site-directed mutagenesis approach by substitution of Ser and Thr residues with Cys at positions 78 and 105 located between two catalytic cysteines. Substitution of Ser with Cys at position 78 enhanced the chaperone activity of the mutant (S78C-PaAhpC) by approximately 9-fold compared with that of the wild-type protein (WT-PaAhpC).

[Case of successful prevention of multiple organ dysfunctions in 74 years old patient with sepsis after Crawford surgery complicated with pleural empyema, chest wall tissues infection and osteomyelitis of ribs].

The article deals with a clinical case demonstrating that patient's elderly age is not an absolute contraindication for complex surgery in spite of high risk of postoperative complications. Early diagnostics, target treatment of the infection cite with vacuum-assisted therapy for wounds and the treatment of infectious complications based on individual characteristics of elderly patient with sepsis as an outcome of prosthetic thoracoabdominal aortic repair allowed avoiding multiple organ dysfunctions in the patient.

Binding mode analyses and pharmacophore model development for stilbene derivatives as a novel and competitive class of α-glucosidase inhibitors.

Stilbene urea derivatives as a novel and competitive class of non-glycosidic α-glucosidase inhibitors are effective for the treatment of type II diabetes and obesity. The main purposes of our molecular modeling study are to explore the most suitable binding poses of stilbene derivatives with analyzing the binding affinity differences and finally to develop a pharmacophore model which would represents critical features responsible for α-glucosidase inhibitory activity. Three-dimensional structure of S.