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Chemical Communications (Cambridge,... Dec 2023Despite the broad utility of ketones in bioconjugation, few methods exist to introduce them into RNA. Here we develop highly reactive 2'-OH acylating reagents containing...
Despite the broad utility of ketones in bioconjugation, few methods exist to introduce them into RNA. Here we develop highly reactive 2'-OH acylating reagents containing strained-ring ketones, and employ them as versatile labeling handles for RNA.
Topics: Ketones; RNA; Acylation; Indicators and Reagents
PubMed: 38054242
DOI: 10.1039/d3cc05123d -
Carbohydrate Polymers May 2017Within the last decade, acylated polysaccharides have drawn attention, since they find applications in numerous fields as biocompatible and biodegradable amphiphilic...
Within the last decade, acylated polysaccharides have drawn attention, since they find applications in numerous fields as biocompatible and biodegradable amphiphilic compounds. The ability of a CE2 acetyl esterase from Clostridium thermocellum to catalyze acyl transfer to β-glucan and manno-polysaccharides of significant interest was investigated. Initially, screening tests were conducted on aldohexose monosaccharides and disaccharides, exploiting the enzyme's strict regioselectivity at O-6 position. Modified monosaccharides acquired acylation yields from 11 up to 65%, showing preference for small chain acyl donors, while disaccharides exhibited conversion yields from 23 up to 58%, with preference to monoacylation. The transesterification reactions were carried out in two-phase mixtures consisted of water/vinyl esters. Acylation of polysaccharides were confirmed by TLC and FT-IR, while the degree of acylation was determined via an indirect method, estimating a range of acylation from 0.022 to 1.083mmol*g depending on the structure and composition of the target polysaccharide.
Topics: Acetylesterase; Acylation; Clostridium thermocellum; Esterification; Monosaccharides; Polysaccharides; Spectroscopy, Fourier Transform Infrared
PubMed: 28267499
DOI: 10.1016/j.carbpol.2017.01.057 -
Food Chemistry Sep 2022Dicarboxylic acids derived acylated-anthocyanins are common in nature, which can also be obtained by enzymatic acylation of anthocyanins. However, little research have...
Dicarboxylic acids derived acylated-anthocyanins are common in nature, which can also be obtained by enzymatic acylation of anthocyanins. However, little research have focused on the properties of anthocyanins with dicarboxylic acid derivatives due to the complexity of isolation, detection, and identification. In this work, pelargonidin-3-glucoside (Pg3G) was acylated with various dicarboxylic acids. The conversion yields of acylated Pg3G were positively associated with carbon chain lengths of dicarboxylic acids. The primary acylated products were identified as pelargonidin-3-(6″-malonyl) glucoside, pelargonidin-3-(6″-succinyl) glucoside, and pelargonidin-3-(6″-glutaryl) glucoside using LC-MS and NMR. Furthermore, the three acylated Pg3G derivatives exhibited improved thermostability and enhanced lipophilicity compared with Pg3G. The improved thermostability was attributed to the influence of dicarboxylic acids substituent on the distribution of flavylium cation, quinoidal base, hemiketal, cis-chalcone, and trans-chalcone at the equilibrium condition. Overall, our research provided insights about the improved stability and lipophilicity of pelargonidin-3-glucoside following enzymatic acylation with aliphatic dicarboxylic acids.
Topics: Acylation; Anthocyanins; Chalcones; Dicarboxylic Acids; Fatty Acids; Glucosides
PubMed: 35500410
DOI: 10.1016/j.foodchem.2022.133077 -
Methods in Molecular Biology (Clifton,... 2008Palmitoylation or S-acylation is the post-translational attachment of fatty acids to cysteine residues and is common among integral and peripheral mem brane proteins....
Palmitoylation or S-acylation is the post-translational attachment of fatty acids to cysteine residues and is common among integral and peripheral mem brane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells. The exact functions of protein palmitoylation are not well understood. Intrin sically hydrophilic proteins, especially signaling molecules, are anchored by long chain fatty acids to the cytoplasmic face of the plasma membrane. Palmitoylation may also promote targeting to membrane subdomains enriched in glycosphingolip ids and cholesterol or affect protein-protein interactions. This chapter describes (1) a standard protocol for metabolic labeling of palmitoylated proteins and also the procedures to prove a covalent and ester-type linkage of the fatty acids, (2) a simple method to analyze the fatty acid content of S-acylated proteins, (3) two methods to analyze dynamic palmitoylation for a given protein and (4) protocolls to study cell-free palmitoylation of proteins.
Topics: Acylation; DNA; Mutagenesis; Polymerase Chain Reaction; Protein Binding; Proteins
PubMed: 18373257
DOI: 10.1007/978-1-60327-084-7_12 -
Journal of Molecular Biology Aug 2020S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a thioester linkage, is the most prevalent kind of lipid modification of proteins.... (Review)
Review
S-acylation, whereby a fatty acid chain is covalently linked to a cysteine residue by a thioester linkage, is the most prevalent kind of lipid modification of proteins. Thousands of proteins are targets of this post-translational modification, which is catalyzed by a family of eukaryotic integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs). Our knowledge of the repertoire of S-acylated proteins has been rapidly expanding owing to development of the chemoproteomic techniques. There has also been an increasing number of reports in the literature documenting the importance of S-acylation in human physiology and disease. Recently, the first atomic structures of two different DHHC-PATs were determined using X-ray crystallography. This review will focus on the insights gained into the molecular mechanism of DHHC-PATs from these structures and highlight representative data from the biochemical literature that they help explain.
Topics: Acylation; Acyltransferases; Crystallography, X-Ray; Humans; Models, Molecular; Protein Domains; Protein Processing, Post-Translational
PubMed: 32522557
DOI: 10.1016/j.jmb.2020.05.023 -
Current Opinion in Chemical Biology Feb 2016Protein fatty-acylation in eukaryotes has been associated with many fundamental biological processes. However, the diversity, abundance and regulatory mechanisms of... (Review)
Review
Protein fatty-acylation in eukaryotes has been associated with many fundamental biological processes. However, the diversity, abundance and regulatory mechanisms of protein fatty-acylation in vivo remain to be explored. Herein, we review the proteomic analysis of fatty-acylated proteins, with a focus on N-myristoylation and S-palmitoylation. We then highlight major challenges and emerging methods for direct site identification, quantitation, and lipid structure characterization to understand the functions and regulatory mechanisms of fatty-acylated proteins in physiology and disease.
Topics: Acylation; Animals; Fatty Acids; Humans; Protein Processing, Post-Translational; Proteins; Proteomics
PubMed: 26656971
DOI: 10.1016/j.cbpa.2015.11.008 -
Journal of the American Chemical Society May 2016Central topics of carbohydrate chemistry embrace structural modifications of carbohydrates and oligosaccharide synthesis. Both require regioselectively protected...
Central topics of carbohydrate chemistry embrace structural modifications of carbohydrates and oligosaccharide synthesis. Both require regioselectively protected building blocks that are mainly available via indirect multistep procedures. Hence, direct protection methods targeting a specific hydroxy group are demanded. Dual hydrogen bonding will eventually differentiate between differently positioned hydroxy groups. As cyanide is capable of various kinds of hydrogen bonding and as it is a quite strong sterically nondemanding base, regioselective O-acylations should be possible at low temperatures even at sterically congested positions, thus permitting formation and also isolation of the kinetic product. Indeed, 1,2-cis-diols, having an equatorial and an axial hydroxy group, benzoyl cyanide or acetyl cyanide as an acylating agent, and DMAP as a catalyst yield at -78 °C the thermodynamically unfavorable axial O-acylation product; acyl migration is not observed under these conditions. This phenomenon was substantiated with 3,4-O-unproteced galacto- and fucopyranosides and 2,3-O-unprotected mannopyranosides. Even for 3,4,6-O-unprotected galactopyranosides as triols, axial 4-O-acylation is appreciably faster than O-acylation of the primary 6-hydroxy group. The importance of hydrogen bonding for this unusual regioselectivity could be confirmed by NMR studies and DFT calculations, which indicate favorable hydrogen bonding of cyanide to the most acidic axial hydroxy group supported by hydrogen bonding of the equatorial hydroxy group to the axial oxygen. Thus, the "cyanide effect" is due to dual hydrogen bonding of the axial hydroxy group which enhances the nucleophilicity of the respective oxygen atom, permitting an even faster reaction for diols than for mono-ols. In contrast, fluoride as a counterion favors dual hydrogen bonding to both hydroxy groups leading to equatorial O-acylation.
Topics: Acylation; Cyanides; Hydrogen Bonding; Indicators and Reagents; Kinetics; Magnetic Resonance Spectroscopy; Stereoisomerism
PubMed: 27104625
DOI: 10.1021/jacs.6b02454 -
Bioorganic & Medicinal Chemistry Letters Jul 1999Natural prostaglandins (PG) F2alpha and E1 as well as (+)-cloprostenol were regioselectively 11-acylated using Novozym 435 as a catalyst and vinyl acetate as an acyl...
Natural prostaglandins (PG) F2alpha and E1 as well as (+)-cloprostenol were regioselectively 11-acylated using Novozym 435 as a catalyst and vinyl acetate as an acyl donor. Unlike the above compounds the 15-OH group of PGE2 was also acylated with a significant velocity under the same conditions. The enantiospecificity of the lipase-catalysed 11-acetylation of cloprostenol was established by separate treatment of(+)- and (-)-cloprostenols.
Topics: Acylation; Lipase; Magnetic Resonance Spectroscopy; Prostaglandins
PubMed: 10406654
DOI: 10.1016/s0960-894x(99)00295-4 -
Biochemical Society Transactions Apr 2015The discovery of the zDHHC family of S-acyltransferase enzymes has been one of the major breakthroughs in the S-acylation field. Now, more than a decade since their... (Review)
Review
The discovery of the zDHHC family of S-acyltransferase enzymes has been one of the major breakthroughs in the S-acylation field. Now, more than a decade since their discovery, major questions centre on profiling the substrates of individual zDHHC enzymes (there are 24 ZDHHC genes and several hundred S-acylated proteins), defining the mechanisms of enzyme-substrate specificity and unravelling the importance of this enzyme family for cellular physiology and pathology.
Topics: Acylation; Acyltransferases; Humans; Multigene Family; Substrate Specificity
PubMed: 25849920
DOI: 10.1042/BST20140270 -
Life Sciences Dec 2022Short-chain fatty acids (SFCAs) exhibit diverse functions from kidneys to human health and diseases, and also could exert their roles in post-translational modifications... (Review)
Review
Short-chain fatty acids (SFCAs) exhibit diverse functions from kidneys to human health and diseases, and also could exert their roles in post-translational modifications (PTMs). Nowadays, novel short-chain lysine acylations derived from SFCAs have attracted more attentions, including propionylation, butyrylation, 2-hydroxyisobutyrylation, β-hydroxybutyrylation, malonylation, succinylation, crotonylation, glutarylation, lactylation, etc. These acylations have multiple physiological effects on many diseases, which also contribute to kidney pathophysiology. Here, we summarize the role of the currently novel PTMs in the kidneys for human health and diseases.
Topics: Humans; Protein Processing, Post-Translational; Lysine; Acylation; Kidney
PubMed: 36375568
DOI: 10.1016/j.lfs.2022.121188