65846-04-0Relevant articles and documents
Formation of a tris(catecholato) iron(iii) complex with a nature-inspired cyclic peptoid ligand
Oh, Jinyoung,Kang, Dahyun,Hong, Sugyeong,Kim, Sun H.,Choi, Jun-Ho,Seo, Jiwon
supporting information, p. 3459 - 3463 (2021/03/22)
Siderophore-mimicking macrocyclic peptoids were synthesized. Peptoid3with intramolecular hydrogen bonds showed an optimally arranged primary coordination sphere leading to a stable catecholate-iron complex. The tris(catecholato) structure of 3-Fe(iii) was determined with UV-vis, fluorescence, and EPR spectroscopies and DFT calculations. The iron binding affinity was comparable to that of deferoxamine, with enhanced stability upon air exposure.
Proteome-Wide Profiling of Cellular Targets Modified by Dopamine Metabolites Using a Bio-Orthogonally Functionalized Catecholamine
Hurben, Alexander K.,Erber, Luke N.,Tretyakova, Natalia Y.,Doran, Todd M.
, p. 2581 - 2594 (2021/11/27)
Selective death of midbrain dopaminergic neurons is a hallmark pathology of Parkinson's disease (PD), but the molecular mechanisms that initiate the cascade of events resulting in neurodegeneration in PD remain unclear. Compelling evidence suggests that dysregulation of dopamine (DA) induces neuronal stress and damage responses that are operative processes in striatal degeneration preceding PD-like symptoms. Improper DA sequestration to vesicles raises cytosolic DA levels, which is rapidly converted into electrophilic dopaquinone species (DQs) that react readily with protein nucleophiles forming covalent modifications that alter the native structure and function of proteins. These so-called DA-protein adducts (DPAs) have been reported to play a role in neurotoxicity, and their abundance with respect to neurodegeneration has been linked to clinical and pathological features of PD that suggest that they play a causal role in PD pathogenesis. Therefore, characterizing DPAs is a critical first step in understanding the susceptibility of midbrain dopaminergic neurons during PD. To help achieve this goal, we report here a novel DA-mimetic (DAyne) containing a biorthogonal alkyne handle that exhibits a reactivity profile similar to DA in aqueous buffers. By linking DPAs formed with DAyne to a fluorescent reporter molecule, DPAs were visualized in fixed cells and within lysates. DAyne enabled global mapping of cellular proteins affected by DQ modification and their bioactive pathways through enrichment. Our proteomic profiling of DPAs in neuronal SH-SY5Y cells indicates that proteins susceptible to DPA formation are extant throughout the proteome, potentially influencing several diverse biological pathways involved in PD such as endoplasmic reticulum (ER) stress, cytoskeletal instability, proteotoxicity, and clathrin function. We validated that a protein involved in the ER stress pathway, protein disulfide isomerase 3 (PDIA3), which was enriched in our chemoproteomic analysis, is functionally inhibited by DA, providing evidence that dysregulated cellular DA may induce or exacerbate ER stress. Thus, DAyne provided new mechanistic insights into DA toxicity that may be observed during PD by enabling characterization of DPAs generated reproducibly at physiologically relevant quinone exposures. We anticipate our design and application of this reactivity-based probe will be generally applicable for clarifying mechanisms of metabolic quinone toxicity.
Cooperativity of Catechols and Amines in High-Performance Dry/Wet Adhesives
Delparastan, Peyman,Gerst, Matthias,Messersmith, Phillip B.,Ney, Max R.,Tiu, Brylee David B.
supporting information, p. 16616 - 16624 (2020/08/03)
The outstanding adhesive performance of mussel byssal threads has inspired materials scientists over the past few decades. Exploiting the amino-catechol synergy, polymeric pressure-sensitive adhesives (PSAs) have now been synthesized by copolymerizing tra
Development of an iron(II)-catalyzed aerobic catechol cleavage and biomimetic synthesis of betanidin
Guimond, Nicolas,Mayer, Peter,Trauner, Dirk
supporting information, p. 9519 - 9523 (2014/08/18)
An aerobic iron(II)-catalyzed cleavage of catechols was developed. This reaction allows for the preparation of 2-methoxy-2H-pyrans that can be employed as versatile building blocks for synthesis. The utility of this biomimetic oxidative cleavage is featured in the synthesis of betanidin, a natural colorant with antioxidant properties. Cut and paste: An aerobic iron(II)-catalyzed oxidative cleavage of catechol was developed. This reaction allows the preparation of 2H-pyrans that can be employed as versatile building blocks for synthesis. The utility of this biomimetic cleavage is featured in the synthesis of betanidin, the aglycone of red beets' principal colorant and itself a valuable antioxidant (see scheme).
Redox properties of LDH microcrystals coated with a catechol-bearing phosphonate derived from dopamine
De Victoria Rodriguez, Maria,Brunet, Ernesto,Nocchetti, Morena,Presciutti, Federica,Costantino, Ferdinando
, p. 26912 - 26917 (2014/07/21)
The surface of Zn-Al-chloride LDH microcrystals (LDH = Layered Double Hydroxides) was activated by grafting a redox active catechol bearing bis-phosphonate obtained by dopamine derivatization. The obtained phosphonate uniformly coats the LDH crystals surface and the catechol groups are exposed. The redox activity of the catechol was employed for the quick and easy synthesis of Gold NPs, which are supported onto the LDH microcrystal surface. The synthetic procedures and the complete characterization of the hybrid system are reported. This journal is the Partner Organisations 2014.
Method of synthesizing acetonide-protected catechol-containing compounds and intermediates produced therein
-
Page/Page column 26-27, (2012/07/30)
The inventors disclose here a novel, facile approach to the synthesis of acetonide-protected catechol-containing compounds having at least one amine group. In specific embodiments, the invention provides novel methods of synthesizing 3,4-dihydroxyphenylalanine (H-DOPA(acetonide)-OH (6)), Fmoc-protected H-DOPA(acetonide)-OH (Fmoc-DOPA(acetonide)-OH (7)), Fmoc-protected dopamine (Fmoc-dopamine(acetonide) (10)), TFA-protected dopamine (TFA-dopamine(acetonide) (13)) and acetonide-protected 4-(2-aminoethyl)benzene-1,2-diol (acetonide-protected dopamine (14)).
Acetonide protection of dopamine for the synthesis of highly pure N-docosahexaenoyldopamine
Liu, Zhongqiang,Hu, Bi-Huang,Messersmith, Phillip B.
supporting information; experimental part, p. 2403 - 2405 (2010/06/21)
Direct acetonide protection of the catechol of dopamine has proven to be problematic due to the formation of Pictet-Spengler isoquinolines. Here we report an efficient method for acetonide protection of dopamine, allowing the preparation of a dopamine prodrug without complications from the Pictet-Spengler reaction. Acetonide-protected dopamine was first synthesized by pre-protecting the amino group with phthaloyl followed by refluxing with 2,2-dimethoxypropane in the presence of TsOH. Further work demonstrated that Fmoc and trifluoroacetyl were also suitable N-protective groups, while Boc-protected dopamine gave an isoquinoline product. Acetonide-protected dopamine was coupled to DHA (all cis-4,7,10,13,16,19-docosahexaenoic acid) to produce the N-DHA-dopamine prodrug with high purity.
N-Acylcatecholamines and 3,4-Dihydro-6,7-isoquinolinediols from N-Acyl-3,4-dimethoxyphenethylamines
Niederstein, Yvonne,Peter, Martin G.
, p. 1189 - 1194 (2007/10/02)
The N-acetamides 2a and 2e are cleaved with boron tribromide to yield as expected the catechols 3a and 3e whereas, under the same conditions, mixtures of the catechols 3b, 3c, 3f, or 3g and 1-(haloalkyl)dihydroisoquinolines 4
