Molecular modeling and anticholinesterasic activity of novel 2-arylaminocyclohexyl N,N-dimethylcarbamates

This work reports a detailed theoretical and experimental study of the novel isomer series cis- and trans-2-arylaminocyclohexyl N,N-dimethylcarbamates as potential inhibitors of cholinesterases. In vitro inhibition assay by Ellman's method with human blood samples showed that the new carbamates are selective to the inhibition of enzyme butyrylcholinesterase (BuChE) with maximum inhibition of 90% and IC50 of 6 and 8 mmol L-1 for the more actives compounds of the series. Molecular modeling studies point to significant differences for the conformations of the compounds in the active sites of enzymes BuChE and acetylcholinesterase (AChE). The results show that the compounds interact more effectively with the active site of enzyme BuChE since the carbamate group is close to the key residues of the catalytic triad.O presente trabalho reporta um estudo teórico e experimental detalhado das séries inéditas de isômeros cis- e trans-N,N-dimetilcarbamatos de cicloexila 2-arilaminossubstituídos como potenciais inibidores de colinesterases. Os testes de inibição in vitro, realizados através do método de Ellman em amostras de sangue humano, mostraram que os novos carbamatos apresentaram boa seletividade frente à inibição da enzima butirilcolinesterase (BuChE), com um máximo de inibição de 90% e IC50 de 6 e 8 mmol L-1 para os compostos mais ativos da série. Os estudos de modelagem molecular apontaram significantes diferenças entre as orientações destes compostos nos sítios ativos das enzimas BuChE e acetilcolinesterase (AChE). Os resultados mostraram que os compostos interagem de forma mais efetiva com o sítio ativo da enzima BuChE, pois o grupo carbamato está próximo aos resíduos chave da tríade catalítica.17981807Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq

Cholinesterases Inhibition by Novel cis

The present study describes the synthesis, assessment of the anticholinesterase activity and the inhibition type of novel cis- and trans-3-arylaminocyclohexyl N,N-dimethylcarbamates. In vitro inhibition assay by Ellman's method with human blood samples showed that carbamates were selective for butyrylcholinesterase (BuChE) with compound concentration that inhibits 50% of enzyme activity (IC50) between 0.11 and 0.18 mmol L-1. cis- and trans-3-(4-Methoxyphenylamino)cyclohexyl N,N-dimethylcarbamate hydrochloride were the most active for BuChE, showing that the presence of methoxyl group enhanced the anticholinesterase activity. The enzyme kinetics studies indicate a noncompetitive inhibition against acetylcholinesterase (AChE) and mixed type inhibition for BuChE. Molecular modeling studies confirm the ability of carbamates to bind both the active and peripheral sites of the BuChE

Notulae to the Italian alien vascular flora: 8

In this contribution, new data concerning the distribution of vascular flora alien to Italy are presented. It includes new records, confirmations, exclusions, and status changes for Italy or for Italian administrative regions of taxa in the genera Bunias, Calocedrus, Calycanthus, Celosia, Clerodendrum, Convolvulus, Crassula, Cyclamen, Datura, Dicliptera, Eragrostis, Erigeron, Gamochaeta, Gazania, Impatiens, Kolkwitzia, Leucaena, Ludwigia, Medicago, Muscari, Nigella, Oenothera, Opuntia, Paulownia, Petroselinum, Phyllostachys, Physalis, Pseudosasa, Quercus, Reynoutria, Roldana, Saccharum, Sedum, Semiarundinaria, Senecio, Sisyrinchium, Solanum, Sporobolus, Tulipa, Vachellia, Verbena, and Youngia. Nomenclatural and distribution updates published elsewhere are provided as Suppl. material 1