3476-86-6Relevant articles and documents
Chalcone scaffolds as photofunctional hybrid material of indolin-2-one-functionalized siloxy framework for optical sensing of Cu2+
Singh, Gurjaspreet,Kalra, Pooja,Arora, Aanchal,Singh, Akshpreet,Sharma, Geetika,Sanchita,Satija, Pinky
, p. 16902 - 16910 (2018)
Owing to their easy approachability and high degree of structural and functional diversity, many multicomponent reactions such as 1,3-dipolar cycloaddition have been a rich source of conjugated π-systems, functionalised chromophores and active molecules. Despite their high potential for investigation and practical benefits, few products have thus far been scrutinized for their metal sensing abilities. In the present study, indolin-2-one chalcones bearing siloxy molecular systems were synthesized by a [2+3] cycloaddition-based reaction sequence. A designed chemosensor exhibited an optical (absorption spectra) response toward Cu2+ ions in an acetonitrile solution. Different aspects of the sensing phenomena such as selectivity and association constants were studied in detail using UV-vis spectroscopy. The calibration plot was linear (R2 = 0.9966) over a large range of Cu2+ ion concentrations (10 μM). This novel effort has initiated a well-organized method for the efficient improvement of cation sensors with triazole for detecting heavy metal pollutants in environmental and healthcare fields on a large scale.
Discovery of novel indolin-2-one compounds as potent inhibitors of HsClpP for cancer treatment
Song, Rao,Yang, Yang,Huang, Jiasheng,Qiao, Wenliang,Luo, Baozhu,Ju, Yuan,Yang, Tao,Luo, Youfu
, (2021/03/29)
Human caseinolytic protease proteolytic subunit (HsClpP) is a highly conserved serine protease that plays an essential role in cell homeostasis through removal of the damaged and/or misfolded proteins. Recently, due to its critical role in cancer prolifer
Macrocyclic Modalities Combining Peptide Epitopes and Natural Product Fragments
Carbajo, Rodrigo J.,Grossmann, Tom N.,Larsson, Niklas,Lemurell, Malin,Plowright, Alleyn T.,Potowski, Marco,Thavam, Sasikala,Valeur, Eric,Waldmann, Herbert,Dahl, G?ran,Dellsén, Anita,Guéret, Stéphanie M.
supporting information, p. 4904 - 4915 (2020/04/01)
"Hot loop" protein segments have variable structure and conformation and contribute crucially to protein-protein interactions. We describe a new hot loop mimicking modality, termed PepNats, in which natural product (NP)-inspired structures are incorporated as conformation-determining and-restricting structural elements into macrocyclic hot loop-derived peptides. Macrocyclic PepNats representing hot loops of inducible nitric oxide synthase (iNOS) and human agouti-related protein (AGRP) were synthesized on solid support employing macrocyclization by imine formation and subsequent stereoselective 1,3-dipolar cycloaddition as key steps. PepNats derived from the iNOS DINNN hot loop and the AGRP RFF hot spot sequence yielded novel and potent ligands of the SPRY domain-containing SOCS box protein 2 (SPSB2) that binds to iNOS, and selective ligands for AGRP-binding melanocortin (MC) receptors. NP-inspired fragment absolute configuration determines the conformation of the peptide part responsible for binding. These results demonstrate that combination of NP-inspired scaffolds with peptidic epitopes enables identification of novel hot loop mimics with conformationally constrained and biologically relevant structure.
