1582776-38-2Relevant academic research and scientific papers
Singlet oxygen carrier for inhibiting beta-amyloid protein aggregation as well as preparation method and application thereof
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, (2021/11/27)
The invention discloses a singlet oxygen carrier for inhibiting beta-amyloid protein aggregation as well as a preparation method and application thereof, which belongs to the technical field of biological medicines. The singlet oxygen carrier for inhibiting beta-amyloid protein aggregation contains two functional groups, namely a benzothiazole group and a singlet oxygen carrier. The benzothiazole group can be selectively combined with the beta-amyloid protein, so that the targeting property of the system is improved, the aggregation of the beta-amyloid protein is inhibited, and the neurotoxicity caused by the beta-amyloid protein is reduced. The endoperoxide in the system can release singlet oxygen under a certain condition, and the singlet oxygen can oxidize the beta-amyloid protein, so that the aggregation of the beta-amyloid protein is further limited, and the toxicity is reduced. The carrier has dual inhibition effects on beta-amyloid protein, and has application potentials of treating related diseases caused by beta-amyloid protein aggregation and relieving Alzheimer's disease and other diseases.
Dual RXR agonists and RAR antagonists based on the stilbene retinoid scaffold
Martínez, Claudio,Lieb, Michele,álvarez, Susana,Rodríguez-Barrios, Fátima,álvarez, Rosana,Khanwalkar, Harshal,Gronemeyer, Hinrich,De Lera, Angel R.
, p. 533 - 537 (2014/06/09)
Arotinoids containing a C5,C8-diphenylnaphthalene-2-yl ring linked to a (C3-halogenated) benzoic acid via an ethenyl connector (but not the corresponding naphthamides), which are prepared by Horner-Wadsworth-Emmons reaction of naphthaldehydes and benzylphosphonates, display the rather unusual property of being RXR agonists (15-fold induction of the RXR reporter cell line was achieved at 3- to 10-fold lower concentration than 9-cis-retinoic acid) and RAR antagonists as shown by transient transactivation studies. The binding of such bulky ligands suggests that the RXR ligand-binding domain is endowed with some degree of structural elasticity.
