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Organic Letters Apr 2001[reaction: see text]. The reaction of unsubstituted indole with different acylating agents such as acid chlorides, anhydrides, nitriles, and amino acid derivatives in...
[reaction: see text]. The reaction of unsubstituted indole with different acylating agents such as acid chlorides, anhydrides, nitriles, and amino acid derivatives in the presence of Lewis acid is reported.
Topics: Acylation; Aluminum Chloride; Aluminum Compounds; Chlorides; Indoles; Molecular Structure; Polymers; Solvents; Tin Compounds; Titanium
PubMed: 11277781
DOI: No ID Found -
Molecules (Basel, Switzerland) Sep 2022Until now, the intermediate responsible for the acyl transfer of a highly enantioselective tetrapeptide organocatalyst for the kinetic resolution of...
Until now, the intermediate responsible for the acyl transfer of a highly enantioselective tetrapeptide organocatalyst for the kinetic resolution of trans-cycloalkane-1,2-diols has never been directly observed. It was proposed computationally that a π-methylhistidine moiety is acylated as an intermediate step in the catalytic cycle. In this study we set out to investigate whether we can detect and characterize this key intermediate using NMR-spectroscopy and mass spectrometry. Different mass spectrometric experiments using a nano-ElectroSpray Ionization (ESI) source and tandem MS-techniques allowed the identification of tetrapeptide acylium ions using different acylation reagents. The complexes of -cyclohexane-1,2-diols with the tetrapeptide were also detected. Additionally, we were able to detect acylated tetrapeptides in solution using NMR-spectroscopy and monitor the acetylation reaction of a -cyclohexane-1,2-diol. These findings are important steps towards the understanding of this highly enantioselective organocatalyst.
Topics: Acylation; Alcohols; Catalysis; Cyclohexanes; Cycloparaffins; Methylhistidines; Peptides; Spectrometry, Mass, Electrospray Ionization; Stereoisomerism
PubMed: 36234884
DOI: 10.3390/molecules27196351 -
Vaccine Dec 2015Covalent attachment of saturated fatty acids (palmitate and stearate) to hemagglutinin (HA) of influenza virus is a protein modification essential for viral replication....
Covalent attachment of saturated fatty acids (palmitate and stearate) to hemagglutinin (HA) of influenza virus is a protein modification essential for viral replication. The enzymes catalysing acylation of viral proteins have not been identified, but likely candidates that acylate cellular substrates are members of a protein family that contain a DHHC (Asp-His-His-Cys) cysteine-rich domain. Since 23 DHHC-proteins with distinct, only partly overlapping substrate specificities are present in humans, only a few of them might acylate HA in airway cells of the lung. We argue here that these DHHC-proteins might be promising drug targets since their blockade should result in suppression of viral replication, while acylation of cellular proteins will not be (or very little) compromised.
Topics: Acylation; Acyltransferases; Animals; Dogs; Fatty Acids; Hemagglutinin Glycoproteins, Influenza Virus; Humans; Lipoylation; Madin Darby Canine Kidney Cells; Mice; Orthomyxoviridae; Palmitic Acid; Stearic Acids; Virus Assembly; Virus Replication
PubMed: 26387429
DOI: 10.1016/j.vaccine.2015.08.095 -
Journal of the American Chemical Society May 1948
Topics: Acylation; Organosilicon Compounds
PubMed: 18861773
DOI: 10.1021/ja01185a035 -
International Journal of Pharmaceutics Jan 2013Acylation of proteins with a fatty acid chain has proven useful for prolonging the plasma half-lives of proteins. In formulation of acylated protein drugs, knowledge...
Acylation of proteins with a fatty acid chain has proven useful for prolonging the plasma half-lives of proteins. In formulation of acylated protein drugs, knowledge about the effect of acylation with fatty acids on the adsorption behaviour of proteins at interfaces will be valuable. The aim of this work was to study the effect of acylation on the adsorption of GLP-2 from aqueous solution to a hydrophobic surface by comparing the adsorption of the 3766 Da GLP-2 with that of a GLP-2 variant acylated with a 16-carbon fatty acid chain through a β-alanine linker. Adsorption of GLP-2 and acylated GLP-2 were studied with isothermal titration calorimetry, fixed-angle optical reflectometry and total internal reflection fluorescence. Furthermore, the effect of acylation of GLP-2 on the secondary structure was studied with Far-UV CD. Acylation was observed to have several effects on the adsorption of GLP-2. Acylation increased the amount of GLP-2 adsorbing per unit surface area and decreased the initial adsorption rate of GLP-2. Finally, acylation increased the strength of the adsorption, as judged by the lower fraction desorbing upon rinsing with buffer.
Topics: Acylation; Adsorption; Glucagon-Like Peptide 2; Hydrophobic and Hydrophilic Interactions; Nanoparticles; Polystyrenes
PubMed: 22310460
DOI: 10.1016/j.ijpharm.2012.01.040 -
Drug Metabolism and Disposition: the... 1985Representative examples of drug metabolites containing a carboxylic acid group conjugated to glucuronic acid are shown to be active chemical electrophiles, which acylate...
Representative examples of drug metabolites containing a carboxylic acid group conjugated to glucuronic acid are shown to be active chemical electrophiles, which acylate albumin in vitro through transesterification reactions. Based on these and other observations, we propose that this acylating reactivity is characteristic of 1-O-acyl glucuronides as a class, and that albumin is representative of many susceptible biopolymers. The hypothesis is advanced that this reaction can occur in vivo as well, and that it may offer a molecular mechanism for the physiological activity or toxicity of some xenobiotic and lipophilic compounds.
Topics: Acylation; Glucuronates; Serum Albumin, Bovine
PubMed: 2861990
DOI: No ID Found -
Current Protocols in Protein Science Feb 2009Proteins can be acylated with a variety of fatty acids attached by different covalent bonds, influencing, among other things, their function and intracellular...
Proteins can be acylated with a variety of fatty acids attached by different covalent bonds, influencing, among other things, their function and intracellular localization. This unit describes methods to analyze protein acylation, both levels of acylation and also the identification of the fatty acid and the type of bond present in the protein of interest. Protocols are provided for metabolic labeling of proteins with tritiated fatty acids, for exploitation of the differential sensitivity to cleavage of different types of bonds, in order to distinguish between them, and for thin-layer chromatography to separate and identify the fatty acids associated with proteins.
Topics: Acylation; Animals; Biochemistry; Cells, Cultured; Chromatography, Thin Layer; Fatty Acids; Humans; Isotope Labeling; Mammals; Protein Binding; Proteins
PubMed: 19235135
DOI: 10.1002/0471140864.ps1402s55 -
The Journal of Biological Chemistry Jul 1985Intact alveolar macrophages were found to acylate alkyl- and acyllysophospholipids with a high selectivity for arachidonate. A specific mechanism appears responsible for...
Intact alveolar macrophages were found to acylate alkyl- and acyllysophospholipids with a high selectivity for arachidonate. A specific mechanism appears responsible for the incorporation of arachidonate into lysophospholipids in intact cells since the kinetic pattern for the formation of the 20:4 species was different from all other species. This specificity was investigated in more detail by examining the enzymatic acylation of 1-alkyl-2-lyso-sn-glycero-3-phosphocholine by macrophage membranes; in the absence of CoA, ATP, and Mg2+, this lysophospholipid was acylated with a high preference for arachidonate that was independent of added free fatty acids. The addition of CoA alone increased the rate of acylation of 1-alkyl-2-lyso-sn-glycero-3-phosphocholine, mainly due to an increase in the formation of species other than those containing arachidonate. When CoA, ATP, and Mg2+ were present, the macrophage membranes catalyzed the acylation of 1-alkyl-2-lyso-sn-glycero-3-phosphocholine without preference for arachidonate. A different apparent Km and Vmax was observed for reactions involving each cofactor condition. We conclude that the acylation of alkyl- and acyllysophospholipids by rabbit alveolar macrophages occurs by three separate mechanisms: a CoA-independent transacylation, a CoA-dependent transacylation (reverse reaction catalyzed by acyl-CoA acyltransferase), and an acyl-CoA-dependent acylation. The CoA-independent transacylation reaction is unique in that it is specific for arachidonate and accounts for the selective acylation of alkyl- and acyllysophospholipids by arachidonate in membrane preparations of alveolar macrophages. This reaction appears to be extremely important in the remodeling of phospholipid molecular species and the mobilization of arachidonate into ether-linked lipids. The transfer of arachidonate to 1-alkyl-2-lyso-sn-glycero-3-phosphocholine also is of importance in the final inactivation step for platelet activating factor (1-alkyl-2-acetyl-sn-glycero-3-phosphocholine), whereby 1-alkyl-2-arachidonoyl-sn-glycerol-3-phosphocholine (a stored precursor of both platelet activating factor and arachidonic acid metabolites) is formed.
Topics: Acylation; Animals; Chromatography, High Pressure Liquid; Coenzyme A; Female; Kinetics; Linoleic Acid; Linoleic Acids; Lysophospholipids; Macrophages; Models, Chemical; Phospholipids; Pulmonary Alveoli; Rabbits
PubMed: 4008481
DOI: No ID Found -
Current Opinion in Structural Biology Dec 2018Histone post-translational modifications are crucial epigenetic mechanisms regulating a variety of biological events. Besides histone lysine acetylation, a repertoire of... (Review)
Review
Histone post-translational modifications are crucial epigenetic mechanisms regulating a variety of biological events. Besides histone lysine acetylation, a repertoire of acylation types have been identified, including formylation, propionylation, butyrylation, crotonylation, 2-hydroxyisobutyrylation, β-hydroxybutyrylation, succinylation, malonylation, glutarylation and benzoylation. From a structural perspective, here we summarize the writers and erasers of histone acylations and explain the molecular basis of these enzymes catalyzing non-acetyl histone acylations with a focus on histone crotonylation and β-hydroxybutyrylation. Histone acylation readout, non-histone acylations and metabolic regulation are also discussed in this review.
Topics: Acylation; Animals; Histone Acetyltransferases; Histone Deacetylases; Histones; Humans; Multienzyme Complexes; Protein Domains; Protein Processing, Post-Translational; Substrate Specificity
PubMed: 30391813
DOI: 10.1016/j.sbi.2018.10.001 -
Journal of Pharmaceutical Sciences Aug 1975The acylation of ascorbic acid by acetic anhydride was studied in water at 25 degrees. The results indicate that the initial products of reactions between these two...
The acylation of ascorbic acid by acetic anhydride was studied in water at 25 degrees. The results indicate that the initial products of reactions between these two compounds were acetic acid and 3-o-acetylascorbic acid. The latter product then underwent two parallel reactions: hydrolysis to ascorbic and acetic acids and an intramolecular O leads to O acyl migration to yield-O-acetylascorbic acid. The former reaction was predominant at pH values below 4, whereas the latter reaction predominated at pH values between 4 and 7. These results are used as a basis for questioning the structural assignments previously made to some ascorbic acid esters.
Topics: Acetylation; Acylation; Anhydrides; Ascorbic Acid; Kinetics; Magnetic Resonance Spectroscopy; Mass Spectrometry; Optical Rotation; Spectrophotometry, Ultraviolet; Water
PubMed: 1151701
DOI: 10.1002/jps.2600640808