68274-83-9Relevant articles and documents
Synthesis of haminol-A and haminol-B, polyenic alarm pheromones of Cephalaspidean molluscs
Alvarez, Rosana,De Lera, Angel R.
, p. 3065 - 3072 (1998)
Two stereocontrolled palladium-catalyzed cross-couplings of 1-alkenyl boronic acids and aryl/alkenyl halides (the Suzuki-Miyaura reaction) are the key steps in an enantioselective approach to the polyene fragment of haminols A and B, alarm pheromones isolated from Haminoea navicula, a Cephalaspidean Opisthobranch mollusc. Chirality rested on the use of (S)-propylene oxide as the starting material.
Synthesis of triphenylphosphonium Vitamin E derivatives as mitochondria-targeted antioxidants
Jameson, Victoria J.A.,Cochemé, Helena M.,Logan, Angela,Hanton, Lyall R.,Smith, Robin A.J.,Murphy, Michael P.
supporting information, p. 8444 - 8453 (2015/10/12)
A series of mitochondria-targeted antioxidants comprising a lipophilic triphenylphosphonium cation attached to the antioxidant chroman moiety of vitamin E by an alkyl linker have been prepared. The synthesis of a series of mitochondria-targeted vitamin E derivatives with a range of alkyl linkers gave compounds of different hydrophobicities. This work will enable the dependence of antioxidant defence on hydrophobicity to be determined in vivo.
Synthesis of a potent photoreactive acidic γ-secretase modulator for target identification in cells
Rennhack, Andreas,Jumpertz, Thorsten,Ness, Julia,Baches, Sandra,Pietrzik, Claus U.,Weggen, Sascha,Bulic, Bruno
, p. 6523 - 6532 (2013/01/14)
Supramolecular self-assembly of amyloidogenic peptides is closely associated with numerous pathological conditions. For instance, Alzheime?s disease (AD) is characterized by abundant amyloid plaques originating from the proteolytic cleavage of the amyloid precursor protein (APP) by β- and γ-secretases. Compounds named γ-secretase modulators (GSMs) can shift the substrate cleavage specificity of γ-secretase toward the production of non-amyloidogenic, shorter Aβ fragments. Herein, we describe the synthesis of highly potent acidic GSMs, equipped with a photoreactive diazirine moiety for photoaffinity labeling. The probes labeled the N-terminal fragment of presenilin (the catalytic subunit of γ-secretase), supporting a mode of action involving binding to γ-secretase. This fundamental step toward the elucidation of the molecular mechanism governing the GSM-induced shift in γ-secretase proteolytic specificity should pave the way for the development of improved drugs against AD.
