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Journal of Agricultural and Food... Mar 2023The goal of this study was to expand the applications of bamboo leaf flavonoids (BLFs) by improving their lipophilicity through enzymatic acylation with vinyl cinnamate....
The goal of this study was to expand the applications of bamboo leaf flavonoids (BLFs) by improving their lipophilicity through enzymatic acylation with vinyl cinnamate. Characterization of the acylated BLFs using Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, high-resolution electrospray ionization mass spectrometry, electrospray ionization with tandem mass spectrometry, and H nuclear magnetic resonance spectroscopy indicated that acylation occurred at the C6-OH position of glucoside moieties. The highest degree of acylation (18.61%) was obtained by reacting BLFs with vinyl cinnamate (1:5, w/w) at 60 °C for 48 h. Acylation significantly improved the lipophilicity of BLFs and their capacity to inhibit lipid peroxidation, as evidenced by the reduced production of lipid hydroperoxides and malondialdehyde in rapeseed oil and rapeseed oil-in-water emulsions during storage at 37 °C for 15 days. The study findings provide important data that will enable the use of BLFs in lipid or lipophilic matrices, such as oil-based foods.
Topics: Antioxidants; Flavonoids; Rapeseed Oil; Acylation; Plant Leaves
PubMed: 36935587
DOI: 10.1021/acs.jafc.2c07673 -
Food Chemistry Jun 2023The instability of lutein has limited its wide application especially in the food industry. In this study, enzymatic acylation of lutein with divinyl adipate was...
The instability of lutein has limited its wide application especially in the food industry. In this study, enzymatic acylation of lutein with divinyl adipate was investigated. Three new acylated lutein derivatives, lutein-3-O-adipate (compound 1), lutein-3'-O-adipate (compound 2) and lutein-di-adipate (compound 3), were identified and their stabilities and bioactivates were evaluated. Notably, compounds 1-3 showed better thermal, light stability and stronger scavenging capacity to ABTS radical cation (ABTS) and hydroxyl radical (OH). Most importantly, these acylated lutein derivatives exhibited excellent protective effects on L-O2 cells upon hydrogen peroxide (HO)-induced oxidative stress. In particular, the acylated lutein derivative termed compound 3 prevented cellular oxidative stress via restraining the overproduction of reactive oxygen species (ROS), thereby increasing related antioxidant enzymes activity and inhibiting apoptosis by mitochondria pathway. Our research provides important insights into the application of acylated lutein derivatives in food, cosmetic, and pharmaceutical products.
Topics: Hydrogen Peroxide; Lutein; Oxidative Stress; Antioxidants; Acylation
PubMed: 36621337
DOI: 10.1016/j.foodchem.2023.135393 -
ChemSusChem 2009Molecular sieves are highly active and selective catalysts with industrial potential for acylation reactions. Zeolites are the catalysts of choice when shape selectivity... (Review)
Review
Molecular sieves are highly active and selective catalysts with industrial potential for acylation reactions. Zeolites are the catalysts of choice when shape selectivity influences the preferential formation of some products, while high conversions are achieved over mesoporous catalysts with enhanced diffusion rates of reactants and products. In this Minireview, we focus on the understanding of the relationship among the structure of molecular sieve, type and concentration of acid sites and activity/selectivity in various acylations of aromatic and olefinic hydrocarbons. The products of these acylation reactions are important compounds for the pharmaceutical industry, fragrance and flavor materials, dyes, polymers, agrochemicals, and other applications.
Topics: Acylation; Calcium Compounds; Catalysis; Green Chemistry Technology; Organic Chemistry Phenomena; Silicates; Zeolites
PubMed: 19350610
DOI: 10.1002/cssc.200900007 -
Journal of Food Science Dec 2021Lutein was enzymatically acylated with saturated fatty acid vinyl esters of different lengths of carbon chain (C -C ) under the action of Candida antarctica lipase B...
Enzymatic acylation of lutein with a series of saturated fatty acid vinyl esters and the thermal stability and anti-lipid oxidation properties of the acylated derivatives.
Lutein was enzymatically acylated with saturated fatty acid vinyl esters of different lengths of carbon chain (C -C ) under the action of Candida antarctica lipase B (Novozyme 435). The acylation reaction was optimized by considering substrate molar ratio, reaction solvent, type of enzyme, and reaction time. The highest yield (88%) was obtained using the Novozyme 435 to catalyze the acylation reaction of lutein and vinyl decanoate (lutein/vinyl decanoate molar ratio of 1/10) for 16 h in methyl tert-butyl ether. Ten lutein esters were synthesized, isolated, and purified, which were characterized by Fourier-transform infrared spectroscopy, high-resolution mass spectrometry, and nuclear magnetic resonance spectroscopy. We found that the acylation of lutein improved its antioxidant capacity in lipid system and thermal stability. Our study extended the potential application of lutein in lipophilic food, cosmetic, and pharmaceutical industries. Practical Application: Enzyme acylation of lutein improved its antioxidant capacity in lipid system and thermal stability, extended its potential application in food, cosmetic, and pharmaceutical industries. In addition, our study also provided a new perspective and cognition for the further development and utilization of lutein.
Topics: Acylation; Esters; Fatty Acids; Lutein
PubMed: 34796492
DOI: 10.1111/1750-3841.15966 -
Bioorganic & Medicinal Chemistry Letters Jun 2017SHAPE chemistry (selective 2'-hydroxyl acylation analyzed by primer extension) has been developed to specifically target flexible nucleotides (often unpaired...
SHAPE chemistry (selective 2'-hydroxyl acylation analyzed by primer extension) has been developed to specifically target flexible nucleotides (often unpaired nucleotides) independently to their purine or pyrimidine nature for RNA secondary structure determination. However, to the best of our knowledge, the structure of 2'-O-acylation products has never been confirmed by NMR or X-ray data. We have realized the acylation reactions between cNMP and NMIA under SHAPE chemistry conditions and identified the acylation products using standard NMR spectroscopy and LC-MS/MS experiments. For cAMP and cGMP, the major acylation product is the 2'-O-acylated compound (>99%). A trace amount of N-acylated cAMP has also been identified by LC-UV-MS. While for cCMP, the isolated acylation products are composed of 96% of 2'-O-acylated, 4% of N,O-diacylated, and trace amount of N-acylated compounds. In addition, the characterization of the major 2'-O-acylated compound by NMR showed slight differences in the conformation of the acylated sugar between the three cyclic nucleotides. This interesting result should be useful to explain some unexpected reactivity of the SHAPE chemistry.
Topics: Acylation; Magnetic Resonance Spectroscopy; Nitrosamines; Nucleic Acid Conformation; Nucleotides; RNA; Tandem Mass Spectrometry
PubMed: 28400233
DOI: 10.1016/j.bmcl.2017.03.096 -
Scientific Reports Nov 2020Acyl-CoAs are reactive metabolites that can non-enzymatically S-acylate and N-acylate protein cysteine and lysine residues, respectively. N-acylation is irreversible and...
Acyl-CoAs are reactive metabolites that can non-enzymatically S-acylate and N-acylate protein cysteine and lysine residues, respectively. N-acylation is irreversible and enhanced if a nearby cysteine residue undergoes an initial reversible S-acylation, as proximity leads to rapid S → N-transfer of the acyl moiety. We reasoned that protein-bound acyl-CoA could also facilitate S → N-transfer of acyl groups to proximal lysine residues. Furthermore, as CoA contains an ADP backbone this may extend beyond CoA-binding sites and include abundant Rossmann-fold motifs that bind the ADP moiety of NADH, NADPH, FADH and ATP. Here, we show that excess nucleotides decrease protein lysine N-acetylation in vitro. Furthermore, by generating modelled structures of proteins N-acetylated in mouse liver, we show that proximity to a nucleotide-binding site increases the risk of N-acetylation and identify where nucleotide binding could enhance N-acylation in vivo. Finally, using glutamate dehydrogenase as a case study, we observe increased in vitro lysine N-malonylation by malonyl-CoA near nucleotide-binding sites which overlaps with in vivo N-acetylation and N-succinylation. Furthermore, excess NADPH, GTP and ADP greatly diminish N-malonylation near their nucleotide-binding sites, but not at distant lysine residues. Thus, lysine N-acylation by acyl-CoAs is enhanced by nucleotide-binding sites and may contribute to higher stoichiometry protein N-acylation in vivo.
Topics: Acetylation; Acylation; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Binding Sites; Flavin-Adenine Dinucleotide; Lysine; NAD; Nucleotides
PubMed: 33219268
DOI: 10.1038/s41598-020-77261-1 -
Journal of Cell Science Oct 2018STX19 is an unusual Q-SNARE as it lacks a C-terminal transmembrane domain. However, it is efficiently targeted to post-Golgi membranes. Here, we set out to determine the...
STX19 is an unusual Q-SNARE as it lacks a C-terminal transmembrane domain. However, it is efficiently targeted to post-Golgi membranes. Here, we set out to determine the intracellular localisation of endogenous STX19 and elucidate the mechanism by which it is targeted to membranes. We have found that a pool of STX19 is localised to tubular recycling endosomes where it colocalises with MICAL-L1 and Rab8 (which has Rab8a and Rab8b forms). Using a combination of genetic, biochemical and cell-based approaches, we have identified that STX19 is S-acylated at its C-terminus and is a substrate for several Golgi-localised S-acyltransferases, suggesting that STX19 is initially S-acylated at the Golgi before trafficking to the plasma membrane and endosomes. Surprisingly, we have found that S-acylation is a key determinant in targeting STX19 to tubular recycling endosomes, suggesting that S-acylation may play a general role in directing proteins to this compartment. In addition, S-acylation also protects STX19 from proteosomal degradation, indicating that S-acylation regulates the function of STX19 at multiple levels.This article has an associated First Person interview with the first author of the paper.
Topics: Acylation; Humans; Protein Transport; Q-SNARE Proteins
PubMed: 30254024
DOI: 10.1242/jcs.212498 -
Vaccine Jul 2022Modification of the 3-glucuronic acid (GlcA) residue from the Quillaja saponin (QS) adjuvants by N-acylation, yields derivatives with linear alkylamides that show...
Modification of the 3-glucuronic acid (GlcA) residue from the Quillaja saponin (QS) adjuvants by N-acylation, yields derivatives with linear alkylamides that show structural and functional changes. Structural, since the relatively unreactive added hydrophobic alkyl chains may modify these glycosides' conformation and micellar structure. Functional, because altering the availability of proposed pharmacophores, like fucose (Fucp) and aldehyde groups, to interact with their cellular receptors, may change these glycosides' adjuvanticity. While deacylated QS (DS-QS) adjuvants bias the response toward a sole anti-inflammatory Th2 immunity against an antigen, their N-alkylated derivatives carrying octyl to dodecylamide residues, modify that response to a pro-inflammatory Th1 immunity. As shown by their IgG2a/IgG1 titer ratios, which are higher than those for Th2 immunity. A result of the fact that in mice, the IgG2a levels are dependent on the direct influence of secreted interferon-γ (IFN-γ), a crucial Th1 cytokine. But addition of the longer and more lipophilic tetradecylamide group, yields derivatives that like DS-QS induce Th2 immunity, as shown by their low IgG2a/IgG1 ratio. Results that imply that changes in these analogs' conformation and micellar structure, would affect the immunomodulatory properties or adjuvanticity of N-acylated DS-QS. Physical changes that may alter the availability of groups like Fucp, to bind to its presumed dendritic cells' lectin receptor DC-SIGN; an essential step in the stimulation of Th2 immunity. Structural properties that in an aqueous environment, would depend on these glycosides' balance of their hydrophilic and lipophilic moieties (HLB), and the interactions of the newly introduced alkyl chain with the native QS' lipophilic triterpene aglycone and hydrophilic oligosaccharide chains. A situation that would explain these new derivatives' qualitative and quantitative changes in adjuvanticity.
Topics: Acylation; Adjuvants, Immunologic; Animals; Immunoglobulin G; Mice; Quillaja; Quillaja Saponins; Saponins
PubMed: 35688726
DOI: 10.1016/j.vaccine.2022.05.084 -
PloS One 2014Acylation of peptide drugs with fatty acid chains has proven beneficial for prolonging systemic circulation as well as increasing enzymatic stability without disrupting...
BACKGROUND
Acylation of peptide drugs with fatty acid chains has proven beneficial for prolonging systemic circulation as well as increasing enzymatic stability without disrupting biological potency. Acylation has furthermore been shown to increase interactions with the lipid membranes of mammalian cells. The extent to which such interactions hinder or benefit delivery of acylated peptide drugs across cellular barriers such as the intestinal epithelia is currently unknown. The present study investigates the effect of acylating peptide drugs from a drug delivery perspective.
PURPOSE
We hypothesize that the membrane interaction is an important parameter for intestinal translocation, which may be used to optimize the acylation chain length for intestinal permeation. This work aims to characterize acylated analogues of the intestinotrophic Glucagon-like peptide-2 by systematically increasing acyl chain length, in order to elucidate its influence on membrane interaction and intestinal cell translocation in vitro.
RESULTS
Peptide self-association and binding to both model lipid and cell membranes was found to increase gradually with acyl chain length, whereas translocation across Caco-2 cells depended non-linearly on chain length. Short and medium acyl chains increased translocation compared to the native peptide, but long chain acylation displayed no improvement in translocation. Co-administration of a paracellular absorption enhancer was found to increase translocation irrespective of acyl chain length, whereas a transcellular enhancer displayed increased synergy with the long chain acylation.
CONCLUSIONS
These results show that membrane interactions play a prominent role during intestinal translocation of an acylated peptide. Acylation benefits permeation for shorter and medium chains due to increased membrane interactions, however, for longer chains insertion in the membrane becomes dominant and hinders translocation, i.e. the peptides get 'stuck' in the cell membrane. Applying a transcellular absorption enhancer increases the dynamics of membrane insertion and detachment by fluidizing the membrane, thus facilitating its effects primarily on membrane associated peptides.
Topics: Acylation; Amino Acid Sequence; Caco-2 Cells; Cell Membrane; Glucagon-Like Peptide 2; Glucagon-Like Peptide-2 Receptor; Humans; Intestinal Absorption; Intestinal Mucosa; Intestines; Molecular Sequence Data; Permeability; Protein Binding; Protein Transport; Receptors, Glucagon
PubMed: 25295731
DOI: 10.1371/journal.pone.0109939 -
Chemical & Pharmaceutical Bulletin Jul 2016Organocatalytic site-selective diversification of 10-deacetylbaccatin III, a key natural product for the semisynthesis of taxol, has been achieved. Various acyl groups...
Organocatalytic site-selective diversification of 10-deacetylbaccatin III, a key natural product for the semisynthesis of taxol, has been achieved. Various acyl groups were selectively introduced into the C(10)-OH of 10-deacetylbaccatin III. The C(10)-OH selective acylation was also applied to acylative site-selective dimerization of 10-deacetylbaccatin III to provide the structurally defined dimer.
Topics: 4-Aminopyridine; Acylation; Catalysis; Molecular Conformation; Taxoids
PubMed: 26903156
DOI: 10.1248/cpb.c16-00037