ß-Casein hydrolysate generated by the cell envelope-associated proteinase of Lactobacillus delbrueckii ssp. lactis CRL 581 protects against trinitrobenzene sulfonic acid-induced colitis in mice.

Lactobacillus delbrueckii ssp. lactis CRL 581, a thermophilic lactic acid bacterium used as a starter culture for the manufacture of several fermented dairy products, possesses an efficient proteolytic system that is able to release a series of potentially bioactive peptides (i.e., antihypertensive and phosphopeptides) from α- and ß-caseins. Considering the potential beneficial health effects of the peptides released by L. delbrueckii ssp. lactis CRL 581 from milk proteins, the aim of this work was to analyze the anti-mutagenic and anti-inflammatory properties of the casein hydrolysates generated by the cell envelope-associated proteinase of this bacterium. The ability of α- and ß-casein hydrolysates to suppress the mutagenesis of a direct-acting mutagen 4-nitroquinoline-N-oxide on Salmonella typhimurium TA 98 and TA 100 increased concomitantly with the time of casein hydrolysis. The anti-inflammatory effect of the ß-casein hydrolysate was evaluated using a trinitrobenzene sulfonic acid (TNBS)-induced Crohn's disease murine model. The hydrolysate was administered to mice 10 d before the intrarectal inoculation of TNBS. The mice that received ß-casein hydrolysate previously to TNBS showed decreased mortality rates, faster recovery of initial body weight loss, less microbial translocation to the liver, decreased ß-glucuronidase and myeloperoxidase activities in the gut, and decreased colonic macroscopic and microscopic damage compared with the animals that did not receive this hydrolysate. In addition, ß-casein hydrolysate exerted a beneficial effect on acute intestinal inflammation by increased interleukin 10 and decreased IFN-γ production in the gut. Our findings are consistent with the health-promoting attributes of the milk products fermented by L. delbrueckii ssp. lactis CRL 581 and open up new opportunities for developing novel functional foods.

Silver nanoparticle-protein interactions and the role of lysozyme as an antagonistic antibacterial agent.

The photoreductive synthesis and antibacterial activity of silver nanoparticles (AgNP) prepared in the presence of bovine serum albumin (BSA) and lysozyme (LZ) were evaluated. AgNP@BSA showed similar antibacterial activity to those stabilized with citrate (AgNP@CIT) and to an AgNO3 solution, suggesting the releases of Ag+ as the mechanism of death. In contrast, AgNP@LZ solutions showed no activity, although LZ behaves as a moderately antibacterial peptide. Furthermore, the addition of LZ to the AgNP@CIT or AgNP@BSA solutions induced their agglomeration and suppressed their original antibacterial efficacy. This antagonistic antibacterial effect exerted by LZ on AgNPs is associated with electrostatic interactions exerted by LZ. Specific metal-LZ interactions produce a harder protein corona on AgNP@LZ that retains Ag+, while LZ acts as a glue for AgNP@CIT or AgNP@LZ due to its opposite electrical charge, besides strong binding to Ag+avoiding the bactericide effect. Therefore, bactericidal effects of AgNP in biological media may be modulated by specific protein interactions.

Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization.

Singlet molecular oxygen ((1)O2) contributes to protein damage triggering biophysical and biochemical changes that can be related with aging and oxidative stress. Serum albumins, such as bovine serum albumin (BSA), are abundant proteins in blood plasma with different biological functions. This paper presents a kinetic and spectroscopic study of the (1)O2-mediated oxidation of BSA using the tris(2,2'-bipyridine)ruthenium(II) cation [Ru(bpy)3](2+) as sensitizer. BSA quenches efficiently (1)O2 with a total (chemical+physical interaction) rate constant kt(BSA)=7.3(±0.4)×10(8)M(-1)s(-1), where the chemical pathway represented 37% of the interaction. This efficient quenching by BSA indicates the participation of several reactive residues. MALDI-TOF MS analysis of intact BSA confirmed that after oxidation by (1)O2, the mass protein increased the equivalent of 13 oxygen atoms. Time-resolved emission spectra analysis of BSA established that Trp residues were oxidized to N'-formylkynurenine, being the solvent-accessible W134 preferentially oxidized by (1)O2 as compared with the buried W213. MS confirmed oxidation of at least two Tyr residues to form dihydroxyphenylalanine, with a global reactivity towards (1)O2 six-times lower than for Trp residues. Despite the lack of MS evidences, kinetic and chemical analysis also suggested that residues other than Trp and Tyr, e.g. Met, must react with (1)O2. Modeling of the 3D-structure of BSA indicated that the oxidation pattern involves a random distribution of (1)O2 into BSA; allowing also the interaction of (1)O2 with buried residues by its diffusion from the bulk solvent through interconnected internal hydrophilic and hydrophobic grooves.

MR safety in patients with implanted deep brain stimulation systems (DBS).

INTRODUCTION: While it is desirable to perform MRI examinations in patients with deep brain stimulators (DBS), a major safety concern exists regarding the potential for excessive heating secondary to magnetically induced electrical currents. This study was designed to determine the safety of MRI and DBS. METHODS: Standard configurations of DBS systems were tested. In vitro testing was performed using a 1.5-Tesla MR system, a gel-filled phantom, and the body and head RF coils with varying levels of RF energy (SAR). A fluoroptic thermometry system was used to record temperatures. RESULTS: Using the 1.5-T MRI and body RF transmit coil, the temperature changes ranged from 2.5 to 25.3 degrees C. Using the 1.5-T MRI and head RF transmit coil, the temperature changes ranged from 2.3 to 7.1 degrees C. CONCLUSIONS: Excessive heating does occur with certain MR imaging conditions. Under certain conditions determined in this study, patients with DBS may safely undergo anatomical MR imaging. In the future, standardized testing and more comprehensive studies will be needed to ensure the MR safety of neurostimulation systems.