Only a limited number of contact herbicides exist in agricultural production. While systemic herbicides are more efficient also at suboptimum spray coverage with long-lasting weed control, contact herbicides provide several advantages. There is no translocation to fruits or roots of plantation and other crop, low risk for resistance development, and minor risk for spray-drift damage. Besides, synthetic products that often have toxicological or residues issues, natural fatty acids, particularly pelargonic acid (PA), have contact activity and are safer for home and garden use. We recently described a methyl capped polyethylene glycol ester of pelargonic acid (PA-MPEG) that acts independent of acid formation. Both, PA-MPEG and PA are applied at high rates per hectare to achieve excellent weed control. Here, we report about potential additives to increase PA-MPEG efficacy. The herbicidal active, 1-decanol, and the non-phytotoxic alkylated seed oil-based adjuvant, HastenTM, improved performance and outperformed a commercial PA herbicide. Both, PA-MPEG and PA appear to mainly act by the disintegration of bio-membranes besides having effects on transpiration. The main suggested effect is desiccation due to cutting the water continuum at the site of evaporation in the intercellular spaces. The synergistic action of the adjuvant HastenTM and its practical uses are also discussed.

/pdf/mechanistic-aspects-and-effects-of-selected-tank-mix-1d5ytrus.pdf

Mechanistic Aspects and Effects of Selected Tank-Mix Partners on Herbicidal Activity of a Novel Fatty Acid Ester

Acinetobacter baumannii is a Gram-negative organism listed as an urgent threat pathogen by the World Health Organization (WHO). Carbapenem-resistant A. baumannii (CRAB), especially, present therapeutic challenges due to complex mechanisms of resistance to β-lactams. One of the most important mechanisms is the production of β-lactamase enzymes capable of hydrolyzing β-lactam antibiotics. Co-expression of multiple classes of β-lactamases is present in CRAB; therefore, the design and synthesis of “cross-class” inhibitors is an important strategy to preserve the efficacy of currently available antibiotics. To identify new, nonclassical β-lactamase inhibitors, we previously identified a sulfonamidomethaneboronic acid CR167 active against Acinetobacter-derived class C β-lactamases (ADC-7). The compound demonstrated affinity for ADC-7 with a Ki = 160 nM and proved to be able to decrease MIC values of ceftazidime and cefotaxime in different bacterial strains. Herein, we describe the activity of CR167 against other β-lactamases in A. baumannii: the cefepime-hydrolysing class C extended-spectrum β-lactamase (ESAC) ADC-33 and the carbapenem-hydrolyzing OXA-24/40 (class D). These investigations demonstrate CR167 as a valuable cross-class (C and D) inhibitor, and the paper describes our attempts to further improve its activity. Five chiral analogues of CR167 were rationally designed and synthesized. The structures of OXA-24/40 and ADC-33 in complex with CR167 and select chiral analogues were obtained. The structure activity relationships (SARs) are highlighted, offering insights into the main determinants for cross-class C/D inhibitors and impetus for novel drug design.

/pdf/sulfonamidoboronic-acids-as-cross-class-inhibitors-of-an-3qkcanqf.pdf

Sulfonamidoboronic Acids as “Cross-Class” Inhibitors of an Expanded-Spectrum Class C Cephalosporinase, ADC-33, and a Class D Carbapenemase, OXA-24/40: Strategic Compound Design to Combat Resistance in Acinetobacter baumannii

/pdf/discovery-and-development-of-a-novel-sustainable-contact-227bbl19.pdf

Discovery and Development of a Novel Sustainable Contact Herbicide Based on Natural Fatty Acids

β-Lactams are the most widely prescribed class of antibiotics that inhibit penicillin-binding proteins (PBPs), particularly transpeptidases that function in peptidoglycan synthesis. A major mechanism of antibiotic resistance is the production of β-lactamase enzymes, which are capable of hydrolyzing β-lactam antibiotics. There have been many efforts to counter increasing bacterial resistance against β-lactams. These studies have mainly focused on three areas: discovering novel inhibitors against β-lactamases, developing new β-lactams less susceptible to existing resistance mechanisms, and identifying non-β-lactam inhibitors against cell wall transpeptidases. Drug discovery in the β-lactam field has afforded a range of research opportunities for academia. In this review, we summarize the recent new findings on both β-lactamases and cell wall transpeptidases because these two groups of enzymes are evolutionarily and functionally connected. Many efforts to develop new β-lactams have aimed to inhibit both transpeptidases and β-lactamases, while several promising novel β-lactamase inhibitors have shown the potential to be further developed into transpeptidase inhibitors. In addition, the drug discovery progress against each group of enzymes is presented in three aspects: understanding the targets, screening methodology, and new inhibitor chemotypes. This is to offer insights into not only the advancement in this field but also the challenges, opportunities, and resources for future research. In particular, cyclic boronate compounds are now capable of inhibiting all classes of β-lactamases, while the diazabicyclooctane (DBO) series of small molecules has led to not only new β-lactamase inhibitors but potentially a new class of antibiotics by directly targeting PBPs. With the cautiously optimistic successes of a number of new β-lactamase inhibitor chemotypes and many questions remaining to be answered about the structure and function of cell wall transpeptidases, non-β-lactam transpeptidase inhibitors may usher in the next exciting phase of drug discovery in this field.

Drug Discovery in the Field of β-Lactams: An Academic Perspective.

The resistance of Gram-negative bacteria to β-lactam antibiotics is mostly due to deactivation of the antibiotics by bacterial enzymes, β-lactamases. Disclosing the factors regulating β-lactamase activity is vital for developing therapies to combat multidrug-resistant pathogens, such as 

Bacterial Phosphorylation Suppresses Carbapenemase Activity of the Class-D β-Lactamase OXA-24/40 from Acinetobacter baumannii

Novel Adjuvant Blend for In-Can and Tank-Mix Application Potential Combining Sustainability and Performance as Versatile Penetration Enhancer

Conformational flexibility in carbapenem hydrolysis drives substrate specificity of the class D carbapenemase OXA-24/40

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Novel Adjuvant Blend for In-Can and Tank-Mix Application Potential Combining Sustainability and Performance as Versatile Penetration Enhancer

Conformational flexibility in carbapenem hydrolysis drives substrate specificity of the class D carbapenemase OXA-24/40