117255-11-5Relevant articles and documents
Amino acid-derived N-heterocyclic carbene palladium complexes for aqueous phase Suzuki-Miyaura couplings
Steeples, Elliot,Kelling, Alexandra,Schilde, Uwe,Esposito, Davide
, p. 4922 - 4930 (2016)
In this work, three ligands produced from amino acids were synthesized and used to produce five bis- and PEPPSI-type palladium-NHC complexes using a novel synthesis route from sustainable starting materials. Three of these complexes were used as precatalysts in the aqueous-phase Suzuki-Miyaura coupling of various substrates displaying high activity. TEM and mercury poisoning experiments provide evidence for Pd-nanoparticle formation stabilized in water.
Amino acid based imidazolium zwitterions as novel and green corrosion inhibitors for mild steel: Experimental, DFT and MD studies
Srivastava,Haque, Jiyaul,Verma,Singh,Lgaz,Salghi,Quraishi
, p. 340 - 352 (2017)
Three novel amino acids based corrosion inhibitors namely 2-(3-(carboxymethyl)-1H-imidazol-3-ium-1-yl)acetate (AIZ-1), 2-(3-(1-carboxyethyl)-1H-imidazol-3-ium-1-yl)propanoate (AIZ-2) and 2-(3-(1-carboxy-2-phenylethyl)-1H-imidazol-3-ium-1-yl)-3-phenylpropa
Synthesis and characterization of Au(I) and Au(III) complexes containing N-heterocyclic ligands derived from amino acids
Alvarado-Rodríguez, José G.,Cortes-Llamas, Sara A.,Espinosa-Macías, María L.,López-Dellamary-Toral, Fernando A.,Manríquez-González, Ricardo,Peregrina-Lucano, A. Aarón,Rangel-Salas, Irma I.,Reynoso-Esparza, Mario A.
, p. 564 - 571 (2014)
A series of [Au(NHC)2] (1a–4a) complexes supported by NHC ligands derived from glycine, alanine, methionine and phenylalanine (1–4 respectively) were prepared via a direct transmetalation reaction of their respective silver complexes. The Au complexes were characterized by ESI-MS and NMR spectroscopy in solution. These compounds exhibit instability when the solvent is removed; they displayed a strong tendency to form colored solutions in the order 4a > 3a?> 2a > 1a, which is associated with gold nanoparticles. 1a and 2a undergo oxidative addition of elemental bromine, yielding [Au(NHC)2Br2] (1b) for 1a and a mixture of [Au(NHC)2Br2] (2b) and [Au(NHC)Br3] (2c) for 2a. 2b and 2c were characterized by single crystal X-ray diffraction.
Bronsted acidic ionic liquids and their zwitterions: Synthesis, characterization and pKa determination
Fei, Zhaofu,Zhao, Dongbin,Geldbach, Tilmann J.,Scopelliti, Rosario,Dyson, Paul J.
, p. 4886 - 4893 (2004)
Imidazolium chlorides with one or two carboxylic acid substituent groups, 1-methyl-3-alkylcarboxylic acid imidazolium chloride, [Me{(CH2) nCOOH}im]Cl (n = 1, 3), and 1,3-dialkylcarboxylic acid imidazolium chloride, [{(CH2)nCOOH}2im]Cl (n = 1, 3), have been synthesized via their corresponding acid esters. Deprotonation of the carboxylic acid functionalized imidazolium chlorides with triethylamine affords the corresponding zwitterions [Me{(CH2)nCOO}im] (n = 1, 3) and [{(CH2)nCOOH}{(CH2)nCOO}im] (n = 1, 3). Subsequent reaction of the zwitterions with strong acids gives the new imidazolium salts [Me{(CH2)nCOOH}im]X (n = 1, 3; X = BF4, CF3SO3) and [{(CH2) nCOOH}2im]X (n = 1, 3; X = BF4, CF 3SO3), which exhibit melting points as low as -61°C. The solid-state structures of two of the carboxylic acid functionalized imidazolium salts have been determined by single-crystal X-ray diffraction analysis. Extensive hydrogen bonding is present between the chloride and the imidazolium, with eight Cl ··H interactions below 3 A. The pKa values of all the salts, determined by potentiometric titration, lie between 1.33 and 4.59 at 25°C.
“Doubly Orthogonal” Labeling of Peptides and Proteins
Tessier, Romain,Ceballos, Javier,Guidotti, Nora,Simonet-Davin, Raphael,Fierz, Beat,Waser, Jerome
supporting information, p. 2243 - 2263 (2019/08/08)
Herein, we report a cysteine bioconjugation methodology for the introduction of hypervalent iodine compounds onto biomolecules. Ethynylbenziodoxolones (EBXs) engage thiols in small organic molecules and cysteine-containing peptides and proteins in a fast and selective addition onto the alkynyl triple bond, resulting in stable vinylbenziodoxolone hypervalent iodine conjugates. The conjugation occurs at room temperature in an open flask under physiological conditions. The use of an azide-bearing EBX reagent enables a “doubly orthogonal” functionalization of the bioconjugate via strain-release-driven cycloaddition and Suzuki-Miyaura cross-coupling of the vinyl hypervalent iodine bond. We successfully applied the methodology on relevant and complex biomolecules, such as histone proteins. Through single-molecule experiments, we illustrated the potential of this doubly reactive bioconjugate by introducing a triplet-state quencher close to a fluorophore, which extended its lifetime by suppressing photobleaching. This work is therefore expected to find broad applications for peptide and protein functionalization. Understanding the molecular basis of life is essential in the search for new medicines. Chemical biology develops molecular tools for studying biological processes, setting the basis for new diagnostics and therapeutics, and relies heavily on the ability to selectively modify biomolecules. Two approaches have been especially fruitful: (1) selective modification of natural biomolecules and (2) selective reaction between non-natural functionalities in the presence of biomolecules (the so-called orthogonal bioconjugation). In our work, we contribute to both by transferring highly reactive hypervalent iodine reagents to cysteine residues in proteins and peptides. The obtained bioconjugates retain the reactive hypervalent bonds, which can be selectively functionalized via a metal-mediated reaction. Combined with a traditional azide tag, our approach allows a doubly orthogonal functionalization of biomolecules and is hence expected to be highly useful in chemical biology. Chemical biology develops molecular tools for studying biological processes, setting the basis for new diagnostics and therapeutics, and relies heavily on the ability to modify selectively biomolecules. In our work, we introduce hypervalent iodine bonds into peptides and proteins, via functionalization of cysteine, by using unique cyclic reagents developed in our group. The hypervalent bond can then be selectively modified in the presence of both natural and synthetic functional groups, opening new opportunities for applications in chemical biology.
