The potential usage of Caatinga natural products against multi-drug-resistant bacteria.

New sources of antibacterial drugs have become urgent with increasing bacterial resistance. Medicinal plants are attractive sources for antimicrobial compounds with fewer side effects and cheaper obtention. Brazil contains six biomes, including Caatinga, a semi-arid tropical vegetation exclusively from Brazil that contains over thousand vascular plant species. This review presents the potential of using Caatinga plant products to treat multidrug-resistant bacteria. This review used the keywords of antimicrobial resistance, resistance profile, multidrug resistance, Caatinga biome, and pathogenic bacteria to search in Scientific Electronic Library Online, the U.S. National Library of Medicine, and Google Scholar. Plant species as Schinopsis brasiliensis Engl., Annona vepretorum Mart., Croton pulegioides Baill., Myracrondruon urundeuva Allemo, Cereus jamacaru DC., Opuntia ficus-indica L., Bauhinia forficata L., Eucalyptus globulus, Croton sonderianus Muell. Arg., Campomanesia pubescens, and Abarema cochliacarpos showed bacteriostatic activity. Encholirium spectabile Mart., Hymenaea courbaril L., Neoglaziovia variegata Mez, Selaginella convoluta Spring, Encholirium spectabile Mart., Bromelia laciniosa Mart., Hymenaea martiana, Commiphora leptophloeos, and Mimosa tenuiflora presented bactericidal activity. Those extracts inhibited clinical-importance bacteria, such as Staphylococcus aureus, Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, and Acinetobacter baumannii. Therefore, Caatinga biome plants are a valuable source of active biomolecules against pathogenic bacteria, and their therapeutic potential must be further explored.

On the catalytic mechanism of polysaccharide lyases: evidence of His and Tyr involvement in heparin lysis by heparinase I and the role of Ca2+.

The structurally diverse polysaccharide lyase enzymes are distributed from plants to animals but share common catalytic mechanisms. One, heparinase I (F. heparinum), is employed in the production of the major anticoagulant drug, low molecular weight heparin, and is a mainstay of cell surface proteoglycan analysis. We demonstrate that heparinase I specificity and efficiency depend on the cationic form of the substrate. Ca(2+)-heparin, in which α-L-iduronate-2-O-sulfate residues adopt (1)C4 conformation preferentially, is a substrate, while Na(+)-heparin is an inhibitor. His and Tyr residues are identified in the catalytic step and a model based on molecular dynamics and docking is proposed, in which deprotonated His203 initiates ß-elimination by abstracting the C5 proton of the α-L-iduonate-2-O-sulfate residue in the substrate, and protonated Tyr357 provides the donor to the hexosamine leaving group.

A new approach for heparin standardization: combination of scanning UV spectroscopy, nuclear magnetic resonance and principal component analysis.

The year 2007 was marked by widespread adverse clinical responses to heparin use, leading to a global recall of potentially affected heparin batches in 2008. Several analytical methods have since been developed to detect impurities in heparin preparations; however, many are costly and dependent on instrumentation with only limited accessibility. A method based on a simple UV-scanning assay, combined with principal component analysis (PCA), was developed to detect impurities, such as glycosaminoglycans, other complex polysaccharides and aromatic compounds, in heparin preparations. Results were confirmed by NMR spectroscopy. This approach provides an additional, sensitive tool to determine heparin purity and safety, even when NMR spectroscopy failed, requiring only standard laboratory equipment and computing facilities.