Chlorine and its importance in the inactivation of bacteria, can it inactivate viruses?

Sodium hypochlorite (NaClO) and its active ingredient, hypochlorous acid (HClO), are the most widely used chlorine-based disinfectants. HClO is a fast-acting antimicrobial that interacts with many biomolecules, including amino acids, lipids, nucleic acids, and sulfur containing membrane components, causing cell damage. In this review, we present examples of the effectiveness of chlorine in general disinfection procedures to inactivate bacteria and, under some conditions, bacteria in biofilms and viruses.

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Methionine-Specific Staining of Collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005408x ◽

1982 ◽

Vol 40 ◽

pp. 294-295

Author(s):

E.M. Kuhn ◽

K.D. Marenus ◽

M. Beer

Keyword(s):

Amino Acids ◽

Collagen Fibers ◽

Type Iii Collagen ◽

Type I ◽

Electron Microscopic ◽

Good Correspondence ◽

Specific Staining ◽

Type Iii ◽

Different Types ◽

Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

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Antimyotoxic Activity of Synthetic Peptides Derived from Bothrops atrox Snake Gamma Phospholipase A2 Inhibitor Selected by Virtual Screening

Current Topics in Medicinal Chemistry ◽

10.2174/1568026619666190725102812 ◽

2019 ◽

Vol 19 (22) ◽

pp. 1952-1961 ◽

Cited By ~ 1

Author(s):

J.C. Sobrinho ◽

A.F. Francisco ◽

R. Simões-Silva ◽

A.M. Kayano ◽

J.J. Alfonso Ruiz Diaz ◽

...

Keyword(s):

Amino Acids ◽

Molecular Docking ◽

Synthetic Peptides ◽

Cell Damage ◽

Neutralization Assay ◽

Phospholipase Activity ◽

Phospholipases A2 ◽

Catalytically Active ◽

Bothrops Atrox

Background: Several studies have aimed to identify molecules that inhibit the toxic actions of snake venom phospholipases A2 (PLA2s). Studies carried out with PLA2 inhibitors (PLIs) have been shown to be efficient in this assignment. Objective: This work aimed to analyze the interaction of peptides derived from Bothrops atrox PLIγ (atPLIγ) with a PLA2 and to evaluate the ability of these peptides to reduce phospholipase and myotoxic activities. Methods: Peptides were subjected to molecular docking with a homologous Lys49 PLA2 from B. atrox venom modeled by homology. Phospholipase activity neutralization assay was performed with BthTX-II and different ratios of the peptides. A catalytically active and an inactive PLA2 were purified from the B. atrox venom and used together in the in vitro myotoxic activity neutralization experiments with the peptides. Results: The peptides interacted with amino acids near the PLA2 hydrophobic channel and the loop that would be bound to calcium in Asp49 PLA2. They were able to reduce phospholipase activity and peptides DFCHNV and ATHEE reached the highest reduction levels, being these two peptides the best that also interacted in the in silico experiments. The peptides reduced the myotubes cell damage with a highlight for the DFCHNV peptide, which reduced by about 65%. It has been suggested that myotoxic activity reduction is related to the sites occupied in the PLA2 structure, which could corroborate the results observed in molecular docking. Conclusion: This study should contribute to the investigation of the potential of PLIs to inhibit the toxic effects of PLA2s.

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