RESUMO
The genus Meganola Dyar, 1898 is reviewed for Korea, with 12 species, including the new species, Meganola parki Oh Cha, sp. n. Illustrations of adults and genitalia of all the Korean species are provided, with a key to species of Meganola based on the external morphology and male genitalia. All known host plants are provided, some of them newly recorded.
Assuntos
Lepidópteros , Mariposas , Animais , Genitália , Masculino , Plantas , República da CoreiaRESUMO
A series of tripeptide aldehyde inhibitors were synthesized and their inhibitory effect against dengue virus type 2 (DENV2) and West Nile virus (WNV) NS3 protease was evaluated side by side with the aim to discover potent flaviviral protease inhibitors and to examine differences in specificity of the two proteases. The synthesized inhibitors feature a varied N-terminal cap group and side chain modifications of a P2-lysine residue. In general a much stronger inhibitory effect of the tripeptide inhibitors was observed toward WNV protease. The inhibitory concentrations against DENV2 protease were in the micromolar range while they were submicromolar against WNV. The data suggest that a P2-arginine shifts the specificity toward DENV2 protease while WNV protease favors a lysine in the P2 position. Peptides with an extended P2-lysine failed to inhibit DENV2 protease suggesting a size-constrained S2 pocket. Our results generally encourage the investigation of di- and tripeptide aldehydes as inhibitors of DENV and WNV protease.
Assuntos
Vírus da Dengue/efeitos dos fármacos , Oligopeptídeos/farmacologia , Inibidores de Proteases/farmacologia , Proteínas Virais/antagonistas & inibidores , Vírus do Nilo Ocidental/efeitos dos fármacos , Sítios de Ligação , Vírus da Dengue/química , Vírus da Dengue/enzimologia , Vírus da Dengue/genética , Modelos Moleculares , Estrutura Molecular , Oligopeptídeos/síntese química , Oligopeptídeos/química , Peptídeo Hidrolases/química , Peptídeo Hidrolases/metabolismo , Inibidores de Proteases/síntese química , Inibidores de Proteases/química , Ligação Proteica , Relação Estrutura-Atividade , Proteínas Virais/química , Proteínas Virais/metabolismo , Vírus do Nilo Ocidental/química , Vírus do Nilo Ocidental/enzimologia , Vírus do Nilo Ocidental/genéticaRESUMO
Herein, we report the first systematic and unbiased evaluation of the BODIPY fluorophore library against a wide panel of biologically relevant molecules, and discoveries of 2 novel fluorescent probes for BSA and dopamine.
Assuntos
Compostos de Boro/química , Corantes Fluorescentes/química , Animais , Bovinos , Dopamina/química , Soroalbumina Bovina/química , Espectrometria de FluorescênciaRESUMO
The first BODIPY library (BD) was synthesized, and a highly selective glucagon sensor, Glucagon Yellow (BD-105), was discovered by fluorescence image-based screening method. BD library was synthesized via a Knoevenagel-type condensation reaction with 160 benzaldehydes and the 1,3 dimethyl-BODIPY scaffold. Using BD compounds, a fluorescence image-based screening was performed against three cell lines including AlphaTC1 and BetaTC6 cells which secret glucagon and insulin, respectively, and HeLa as control cells. Out of the 160 candidate probes, one compound, Glucagon Yellow, exhibited selective staining only in AlphaTC1 cells. The selectivity of Glucagon Yellow toward glucagon was confirmed in vitro by comparison of its fluorescence intensity change against 19 biologically relevant analytes. Subsequent immunostaining experiments revealed that Glucagon Yellow and the glucagon antibody colocalized in pancreas tissue, showing a high quantitative correlation analysis by the Pearson's coefficient constant (R(r) = 0.950). These results demonstrated the potential application of Glucagon Yellow as a glucagon imaging agent in live cells and tissues.
