2456-73-7Relevant academic research and scientific papers
Preparation of synthetic auxin-amino acid conjugates
Revelou, Panagiota-Kyriaki,Constantinou-Kokotou, Violetta
supporting information, p. 1708 - 1712 (2019/05/15)
Auxin amide conjugates are regulators of the most important auxin, indole-3-acetic acid (IAA), which is considered responsible for many important processes within the plants. Herein, amide conjugates of IAA were synthesized employing a simple and efficient coupling method with WSCI·HCl, a water-soluble condensing reagent, in the presence of 1-hydroxybenzotriazole. IAA conjugates with 10 amino acids along with their corresponding methyl esters were prepared in excellent yields, up to 95%, aiming to facilitate their identification in plant species. Eight IAA-amino acid methyl ester conjugates are characterized here for the first time.
Modification of auxinic phenoxyalkanoic acid herbicides by the acyl acid amido synthetase GH3.15 from Arabidopsis
Sherp, Ashley M.,Lee, Soon Goo,Schraft, Evelyn,Jez, Joseph M.
, p. 17731 - 17738 (2018/12/12)
Herbicide-resistance traits are the most widely used agriculture biotechnology products. Yet, to maintain their effectiveness and to mitigate selection of herbicide-resistant weeds, the discovery of new resistance traits that use different chemical modes of action is essential. In plants, the Gretchen Hagen 3 (GH3) acyl acid amido synthetases catalyze the conjugation of amino acids to jasmonate and auxin phytohormones. This reaction chemistry has not been explored as a possible approach for herbicide modification and inactivation. Here, we examined a set of Arabidopsis GH3 proteins that use the auxins indole-3-acetic acid (IAA) and indole-3-butyric acid (IBA) as substrates along with the corresponding auxinic phenoxyalkanoic acid herbicides 2,4-dichlorophenoxylacetic acid (2,4-D) and 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB). The IBA-specific AtGH3.15 protein displayed high catalytic activity with 2,4-DB, which was comparable to its activity with IBA. Screening of phenoxyalkanoic and phenylalkyl acids indicated that side-chain length of alkanoic and alkyl acids is a key feature of AtGH3.15’s substrate preference. The X-ray crystal structure of the AtGH3.15?2,4-DB complex revealed how the herbicide binds in the active site. In root elongation assays, Arabidopsis AtGH3.15-knockout and -overexpression lines grown in the presence of 2,4-DB exhibited hypersensitivity and tolerance, respectively, indicating that the AtGH3.15-cata-lyzed modification inactivates 2,4-DB. These findings suggest a potential use for AtGH3.15, and perhaps other GH3 proteins, as herbicide-modifying enzymes that employ a mode of action different from those of currently available herbicide-resistance traits.
Therapeutic and diagnostic ligand systems comprising transport molecule binding properties and medicaments containing the same
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, (2008/06/13)
The invention relates to transport molecule binding ligand compounds which comprise a therapeutically and/or diagnostically active substance and a carrier molecule-affine substance with a high association constant to the carrier molecule. The invention also relates to medicaments containing these ligand compounds and to diagnostic kits.
