Malbari, Khushboo D. published the artcileStructure-aided drug development of potential neuraminidase inhibitors against pandemic H1N1 exploring alternate binding mechanism, SDS of cas: 1772-76-5, the publication is Molecular Diversity (2019), 23(4), 927-951, database is CAplus and MEDLINE.
The rate of mutability of pathogenic H1N1 influenza virus is a threat. The emergence of drug resistance to the current competitive inhibitors of neuraminidase, such as oseltamivir and zanamivir, attributes to a need for an alternative approach. The design and synthesis of new analogs with alternate approach are particularly important to identify the potential neuraminidase inhibitors which may not only have better anti-influenza activity but also can withstand challenge of resistance. Five series of scaffolds, namely aurones (1a-1e), pyrimidine analogs (2a-2b), cinnamic acid analogs (3a-3k), chalcones (4a-4h) and cinnamic acid linkages (5a-5c), were designed based on virtual screening against pandemic H1N1 virus. Mol. modeling studies revealed that the designed analogs occupied 430-loop cavity of neuraminidase. Docking of sialic acid in the active site preoccupied with the docked analogs, i.e. in 430-loop cavity, resulted in displacement of sialic acid from its native pose in the catalytic cavity. The favorable analogs were synthesized and evaluated for the cytotoxicity and cytopathic effect inhibition by pandemic H1N1 virus. All the designed analogs resulting in displacement of sialic acid suggested alternate binding mechanism. Overall results indicated that aurones can be measured best among all as potential neuraminidase inhibitor against pandemic H1N1 virus.
Molecular Diversity published new progress about 1772-76-5. 1772-76-5 belongs to catalysis-chemistry, auxiliary class Benzenes, name is (E)-3-(3-Nitrophenyl)acrylic acid, and the molecular formula is C9H7NO4, SDS of cas: 1772-76-5.
Referemce:
https://courses.lumenlearning.com/boundless-chemistry/chapter/catalysis/,
Catalysis – Wikipedia