2459-07-6Relevant articles and documents
A chromone hydrazide Schiff base fluorescence probe with high selectivity and sensitivity for the detection and discrimination of human serum albumin (HSA) and bovine serum albumin (BSA)
Fan, Jing,Li, Qing-Zhong,Li, Zhe,Liu, Hai-Bo,Wang, Zhi-Gang,Xie, Cheng-Zhi,Xu, Jing-Yuan,Yan, Xiao-Jing
, (2021/10/12)
The discrimination and identification of human serum albumin (HSA) and bovine serum albumin (BSA) is very important, which is due to the vital roles of two SAs in biological and pharmaceutical research. Based on structural screening and docking calculation from a series of homologues, a coumarin Schiff base fluorescent probe 3-hydroxy-N′-((4-oxo-4H-chromen-3-yl)methylene)-2-naphthohydrazide (HCNH) has been designed and synthesized, which could effectively discriminate HSA and BSA. The probe HCNH exhibited superior sensitivity toward HSA and BSA with the detection limits of 10.62 nM and 16.03 nM in PBS solution, respectively. The binding mechanism of HCNH with SAs was studied by Job's plot analysis, SA destruction and displacement assay. Molecular docking and DFT methods were utilized to provide deep insight into the spatial conformation change of HCNH and binding sites in HSA/BSA. The conformation of HCNH was significantly influenced by the microenvironment provided by HSA and BSA, therefore its fluorescence emission was affected correspondingly. Non-toxic probe HCNH could be successfully used for fluorescence bio-imaging of HSA in cancer cells, which is significantly different from normal cells and favors the application in medical diagnosis.
Cis and Trans Isomers of Fe(II) and Co(II) Complexes with Oxadiazole Derivatives - Structural and Magnetic Properties
Zoufaly, Pavel,Kliuikov, Andrii,?i?már, Erik,Císa?ová, Ivana,Herchel, Radovan
, p. 1190 - 1199 (2021/03/08)
Four complexes with bidentate N,N-donors 2-(furan-2-yl)-5-(pyridin-2-yl)-1,3,4-oxadiazole (fpo) and 2-(pyridin-2-yl)-5-(thiophen-2-yl)-1,3,4-oxadiazole (pto) with general formula [M(L)2(NCS)2] (M=Co(II), L=fpo for (1); M=Co(II), L=pto for (2); M=Fe(II), L=fpo (3); M=Fe(II), L=pto (4)) are reported. Analysis and characterization of the samples was performed using standard physico-chemical techniques – elemental analysis, nuclear magnetic resonance, Fourier transform infrared spectroscopy, single-crystal X-ray diffraction. Magnetic properties for 1–4 revealed large magnetic anisotropy of Co(II) complexes, and AC susceptibility measurements confirmed their single-molecule magnetic behaviour. Furthermore, the theoretical calculations at DFT and CASSCF/NEVPT2 level of theory were exploited to better understand magnetism of these compounds.
N-acylhydrazones confer inhibitory efficacy against New Delhi metallo-β-lactamase-1
Gao, Han,Li, Jia-Qi,Kang, Peng-Wei,Chigan, Jia-Zhu,Wang, Huan,Liu, Lu,Xu, Yin-Sui,Zhai, Le,Yang, Ke-Wu
, (2021/07/07)
The expression of β-lactamases, especially metallo-β-lactamases (MβLs) in bacteria is one of the main causes of drug resistance. In this work, an effective N-acylhydrazone scaffold as MβL inhibitor was constructed and characterized. The biological activity assays indicated that the synthesized N-acylhydrazones 1–11 preferentially inhibited MβL NDM-1, and 1 was found to be the most effective inhibitor with an IC50 of 1.2 μM. Analysis of IC50 data revealed a structure–activity relationship, which is that the pyridine and hydroxylbenzene substituents at 2-position improved inhibition of the compounds on NDM-1. ITC and enzyme kinetics assays suggested that it reversibly and competitively inhibited NDM-1 (Ki = 0.29 ± 0.05 μM). The synthesized N-acylhydrazones showed synergistic antibacterial activities with meropenem, reduced 4–16-fold MIC of meropenem on NDM-1- producing E. coli BL21 (DE3), while 1 restored 4-fold activity of meropenem on K. pneumonia expressing NDM-1 (NDM-K. pneumoniae). The mice experiments suggested that 1 combined meropenem to fight against NDM-K. pneumoniae infection in the spleen and liver. Cytotoxicity assays showed that 1 and 2 have low cytotoxicity. This study offered a new framework for the development of NDM-1 inhibitors.