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This paper presents a synthesis of the results obtained during a long- -term investigations conducted on the distribution of aphidophagous coccinellid species and their quantitative and qualitative structure in sugar beet fields in Vojvodina. Composition of coccinellid communities and the annual changes in abundance of species are influenced by many variable environmental factors, but also by the prey availability during the season. Chemical treatments against flea beetles in May or/and against noctuid larvae in late July and the type of the adjacent crops may also affect the quantitative composition of adults coccinellid on sugar beet fields. During the season adults coccinellid are more abundant than larvae. The qualitative structure of coccinellid communities in sugar beet fields is not different than those from other field crops. These communities consist mainly of Coccinella septempunctata L.; Semiadalia undecimnotata Schn.; Propylaea quatuordecimpunctata L.; Hippodamia (Adonia) variegata Goeze and Hippodamia tredecimpunctata L. Other species are present in a small fractions.

E1A binding protein (p300) and CREB binding protein (CBP) are two highly homologous and multidomain histone acetyltransferases. These two proteins are involved in many cellular processes by acting as coactivators of a large number of transcription factors. Dysregulation of p300/CBP has been found in a variety of cancers and other diseases, and inhibition has been shown to decrease Myc expression. Herein, we report the identification of a series of highly potent, proline-based small-molecule p300/CBP histone acetyltransferase (HAT) inhibitors using DNA-encoded library technology in combination with high-throughput screening. The strategy of reducing ChromlogD and fluorination of metabolic soft spots was explored to improve the pharmacokinetic properties of potent p300 inhibitors. Fluorination of both cyclobutyl and proline rings of 22 led to not only reduced clearance but also improved cMyc cellular potency.

A novel series of 5,10-dihydro-dibenzo[b,e][1,4]diazepin-11-ones have been synthesized as potent and selective checkpoint kinase 1 (Chk1) inhibitors via structure-based design. Aided by protein X-ray crystallography, medicinal chemistry efforts led to the identification of compound 46d, with potent enzymatic activity against Chk1 kinase. While maintaining a low cytotoxicity of its own, compound 46d exhibited a strong ability to abrogate G2 arrest and increased the cytotoxicity of camptothecin by 19-fold against SW620 cells. Pharmacokinetic studies revealed that it had a moderate bioavailabilty of 20% in mice. Two important binding interactions between compound 46b and Chk1 kinase, revealed by X-ray cocrystal structure, were hydrogen bonds between the hinge region and the amide bond of the core structure and a hydrogen bond between the methoxy group and Lys38 of the protein.