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Background/Introduction: Healthcare worker uniforms are a potential reservoir for microorganisms, and thus contaminated dress may transmit pathogenic organisms in hospital settings. This study aims at isolating the bacteria from traditional dresses used in a tertiary care hospital, Saudi Arabia, and compares them with whitecoat. Also, this study explores the relationship between bacterial contamination and type of department, type of provider specialty, and dress textile material. Methods: A Descriptive Analytic cross-sectional study was conducted. Multiple culture swabs were obtained from these traditional dresses and whitecoats of the healthcare workers and were analyzed for the rate of bacterial contamination. This study also compares the bacterial contamination rates between medical workers and non-medical personnel like the administrative staff. A Sample size of 742 swabs from 139 participants,from multiple sites was obtained.Data analysis was presented as mean± SD, or as median and range according to the type of distribution of each variable. The Chi-square test was used to test for the association and/or difference between two categorical variables and p-value for statistical significance. Results: It was seen that bacterial contamination of 29.7% was seen in traditional dress compared to 22.5% of those wearing Whitecoat. Concerning the type of traditional dress, the highest rate of bacterial contamination was observed with Thop (40%), followed by Niqab (36.1%). Regarding the source textile material, the mixed type had the highest rate of bacterial contamination (35.7%). Conclusion: The traditional dress showed to be higher in the rate of bacterial contamination in comparison to whitecoats. Also, we found that the type of department and type provider specialty concerning bacterial contamination has a no different effect when compared to others. in our results, the administrative staff carries the same results as healthcare workers regarding bacterial contamination highlighting that they can share in the risk of bacterial transmission.

The metallopeptidases thimet oligopeptidase (THOP, EC 3.4.24.25) and neurolysin (NEL, EC 3.4.24.26) are enzymes that belong to the zinc endopeptidase M13 family. Numerous studies suggest that these peptidases participate in the processing of bioactive peptides such as angiotensins and bradykinin. Efforts have been conducted to develop biotechnological tools to make possible the use of both proteases to regulate blood pressure in mice, mainly limited by the low plasmatic stability of the enzymes. In the present study, it was investigated the use of nanotechnology as an efficient strategy for to circumvent the low stability of the proteases. Recombinant THOP and NEL were immobilized in gold nanoparticles (GNPs) synthesized in situ using HEPES and the enzymes as reducing and stabilizing agents. The formation of rTHOP-GNP and rNEL-GNP was characterized by the surface plasmon resonance band, zeta potential and atomic force microscopy. The gain of structural stability and activity of rTHOP and rNEL immobilized on GNPs was demonstrated by assays using fluorogenic substrates. The enzymes were also efficiently immobilized on GNPs fabricated with sodium borohydride. The efficient immobilization of the oligopeptidases in gold nanoparticles with gain of stability may facilitate the use of the enzymes in therapies related to pressure regulation and stroke, and as a tool for studying the physiological and pathological roles of both proteases.

The metallopeptidases thimet oligopeptidase (THOP, EC 3.4.24.25) and neurolysin (NEL, EC 3.4.24.26) are enzymes that belong to the zinc endopeptidase M13 family. Numerous studies suggest that these peptidases participate in the processing of bioactive peptides such as angiotensins and bradykinin. Efforts have been conducted to develop biotechnological tools to make possible the use of both proteases to regulate blood pressure in mice, mainly limited by the low plasmatic stability of the enzymes. In the present study, it was investigated the use of nanotechnology as an efficient strategy for to circumvent the low stability of the proteases. Recombinant THOP and NEL were immobilized in gold nanoparticles (GNPs) synthesized in situ using HEPES and the enzymes as reducing and stabilizing agents. The formation of rTHOP-GNP and rNEL-GNP was characterized by the surface plasmon resonance band, zeta potential and atomic force microscopy. The gain of structural stability and activity of rTHOP and rNEL immobilized on GNPs was demonstrated by assays using fluorogenic substrates. The enzymes were also efficiently immobilized on GNPs fabricated with sodium borohydride. The efficient immobilization of the oligopeptidases in gold nanoparticles with gain of stability may facilitate the use of the enzymes in therapies related to pressure regulation and stroke, and as a tool for studying the physiological and pathological roles of both proteases. [ABSTRACT FROM AUTHOR]