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1.
Polymers (Basel) ; 14(15)2022 Jul 25.
Article in English | MEDLINE | ID: mdl-35893964

ABSTRACT

Soda lignin is a by-product of the soda process for producing cellulose from grassy raw materials. Since a method for the industrial processing of lignin of this type is still lacking, several research teams have been working on solving this problem. We first propose a modification of soda lignin with sulfamic acid over solid catalysts. As solid catalysts for lignin sulfation, modified carbon catalysts (with acid sites) and titanium and aluminum oxides have been used. In the elemental analysis, it is shown that the maximum sulfur content (16.5 wt%) was obtained with the Sibunit-4® catalyst oxidized at 400 °C. The incorporation of a sulfate group has been proven by the elemental analysis and Fourier-transform infrared spectroscopy. The molecular weight distribution has been examined by gel permeation chromatography. It has been demonstrated that the solid catalysts used in the sulfation process causes hydrolysis reactions and reduces the molecular weight and polydispersity index. It has been established by the thermal analysis that sulfated lignin is thermally stabile at temperatures of up to 200 °C. According to the atomic force microscopy data, the surface of the investigated film consists of particles with an average size of 50 nm. The characteristics of the initial and sulfated ß-O-4 lignin model compounds have been calculated and recorded using the density functional theory.

2.
Int J Mol Sci ; 23(3)2022 Jan 29.
Article in English | MEDLINE | ID: mdl-35163526

ABSTRACT

Betulin is an important triterpenoid substance isolated from birch bark, which, together with its sulfates, exhibits important bioactive properties. We report on a newly developed method of betulin sulfation with sulfamic acid in pyridine in the presence of an Amberlyst®15 solid acid catalyst. It has been shown that this catalyst remains stable when being repeatedly (up to four cycles) used and ensures obtaining of sulfated betulin with a sulfur content of ~10%. The introduction of the sulfate group into the betulin molecule has been proven by Fourier-transform infrared, ultraviolet-visible, and nuclear magnetic resonance spectroscopy. The Fourier-transform infrared (FTIR) spectra contain absorption bands at 1249 and 835-841 cm-1; in the UV spectra, the peak intensity decreases; and, in the nuclear magnetic resonance (NMR) spectra, of betulin disulfate, carbons С3 and С28 are completely shifted to the weak-field region (to 88.21 and 67.32 ppm, respectively) with respect to betulin. Using the potentiometric titration method, the product of acidity constants K1 and K2 of a solution of the betulin disulfate H+ form has been found to be 3.86 × 10-6 ± 0.004. It has been demonstrated by the thermal analysis that betulin and the betulin disulfate sodium salt are stable at temperatures of up to 240 and 220 °C, respectively. The density functional theory method has been used to obtain data on the most stable conformations, molecular electrostatic potential, frontier molecular orbitals, and mulliken atomic charges of betulin and betulin disulfate and to calculate the spectral characteristics of initial and sulfated betulin, which agree well with the experimental data.


Subject(s)
Sulfonic Acids/chemistry , Triterpenes/chemistry , Catalysis , Density Functional Theory , Molecular Conformation , Molecular Structure , Quantum Theory , Spectroscopy, Fourier Transform Infrared , X-Ray Diffraction
3.
Foods ; 10(11)2021 Oct 25.
Article in English | MEDLINE | ID: mdl-34828852

ABSTRACT

Xanthan is an important polysaccharide with many beneficial properties. Sulfated xanthan derivatives have anticoagulant and antithrombotic activity. This work proposes a new method for the synthesis of xanthan sulfates using sulfamic acid. Various N-substituted ureas have been investigated as process activators. It was found that urea has the greatest activating ability. BBD of xanthan sulfation process with sulfamic acid in 1,4-dioxane has been carried out. It was shown that the optimal conditions for the sulfation of xanthan (13.1 wt% sulfur content) are: the amount of sulfating complex per 1 g of xanthan is 3.5 mmol, temperature 90 °C, duration 2.3 h. Sulfated xanthan with the maximum sulfur content was analyzed by physicochemical methods. Thus, in the FTIR spectrum of xanthan sulfate, in comparison with the initial xanthanum, absorption bands appear at 1247 cm-1, which corresponds to the vibrations of the sulfate group. It was shown by GPC chromatography that the starting xanthan gum has a bimodal molecular weight distribution of particles, including a high molecular weight fraction with Mw > 1000 kDa and an LMW fraction with Mw < 600 kDa. It was found that the Mw of sulfated xanthan gum has a lower value (~612 kDa) in comparison with the original xanthan gum, and a narrower molecular weight distribution and is characterized by lower PD values. It was shown by thermal analysis that the main decomposition of xanthan sulfate, in contrast to the initial xanthan, occurs in two stages. The DTG curve has two pronounced peaks, with maxima at 226 and 286 °C.

4.
ACS Omega ; 6(35): 22603-22615, 2021 Sep 07.
Article in English | MEDLINE | ID: mdl-34514232

ABSTRACT

Sulfated cellulose derivatives are biologically active substances with anticoagulant properties. In this study, a new sulfated diethylaminoethyl (DEAE)-cellulose derivative has been obtained. The effect of a solvent on the sulfation process has been investigated. It is shown that 1,4-dioxane is the most effective solvent, which ensures the highest sulfur content in DEAE-cellulose sulfate under sulfamic acid sulfation. The processes of sulfamic acid sulfation in the presence of urea in 1,4-dioxane and in a deep eutectic solvent representing a mixture of sulfamic acid and urea have been compared. It is demonstrated that the use of 1,4-dioxane yields the sulfated product with a higher sulfur content. The obtained sulfated DEAE-cellulose derivatives have been analyzed by Fourier transform infrared spectroscopy, X-ray diffractometry, and scanning electron and atomic force microscopy, and the degree of their polymerization has been determined. The introduction of a sulfate group has been confirmed by the Fourier transform infrared spectroscopy data; the absorption bands corresponding to sulfate groups have been observed in the ranges of 1247-1256 and 809-816 cm-1. It is shown that the use of a deep eutectic solvent leads to the side carbamation reactions. Amorphization of DEAE-cellulose during sulfation has been demonstrated using X-ray diffractometry. The geometric structure of a molecule in the ground state has been calculated using the density functional theory with the B3LYP/6-31G(d, p) basis set. The reactive areas of DEAE-cellulose and its sulfated derivatives have been analyzed using molecular electrostatic potential maps. The thermodynamic parameters (heat capacity, entropy, and enthalpy) of the target sulfation products have been determined. The HOMO-LUMO energy gap, Mulliken atomic charges, and electron density topology of the title compound have been calculated within the atoms in molecule theory.

5.
J Mol Model ; 27(1): 5, 2021 Jan 02.
Article in English | MEDLINE | ID: mdl-33389146

ABSTRACT

The synthesis of guar gum sulfates by a complex of sulfur trioxide with 1,4-dioxane was studied. The influence of temperature, process duration, and the volume of chlorosulfonic acid on the degree of substitution of guar gum sulfates was studied. The sulfation process has been optimized using the Box-Behnken design. It was shown that the optimal conditions for sulfation of guar gum with a complex of sulfur trioxide-1.4-dioxane: temperature 60 °C, duration 2.9 h, and a volume of chlorosulfonic acid of 3.1 ml. Sulfate groups embedding into the structure of guar gum was confirmed by elemental analysis and FTIR. The initial and sulfated guar gum were also characterized by methods: X-ray diffraction, scanning electron microscopy, and gel permeation chromatography. Using X-ray diffraction, it was shown that amorphization of guar gum occurs during sulfation. Using scanning electron microscopy, it was shown that the morphology of guar gum changes in the process of sulfation. Using gel permeation chromatography, it was shown in the process of guar gum sulfation by a complex of sulfur trioxide with 1,4-dioxane, the molecular weight decreases from 600 to 176 kDa. The geometric parameters of all complexes were carried out by using the DFT/B3PW91 method with a 6-31 + G (d,p) basis set. These structures are optimized to predict the important properties of a theme. MEP with contour map has been performed to obtain the electronic properties. Frontier molecular orbital HOMO-LUMO orbital diagram has been obtained for different energy levels and their band gap energies have been computed.

6.
J Biol Chem ; 281(6): 3198-203, 2006 Feb 10.
Article in English | MEDLINE | ID: mdl-16339146

ABSTRACT

Viruses require specific cellular receptors to infect their target cells. Angiotensin-converting enzyme 2 (ACE2) is a cellular receptor for two divergent coronaviruses, SARS coronavirus (SARS-CoV) and human coronavirus NL63 (HCoV-NL63). In addition to hostcell receptors, lysosomal cysteine proteases are required for productive infection by some viruses. Here we show that SARS-CoV, but not HCoV-NL63, utilizes the enzymatic activity of the cysteine protease cathepsin L to infect ACE2-expressing cells. Inhibitors of cathepsin L blocked infection by SARS-CoV and by a retrovirus pseudotyped with the SARS-CoV spike (S) protein but not infection by HCoV-NL63 or a retrovirus pseudotyped with the HCoV-NL63 S protein. Expression of exogenous cathepsin L substantially enhanced infection mediated by the SARS-CoV S protein and by filovirus GP proteins but not by the HCoV-NL63 S protein or the vesicular stomatitis virus G protein. Finally, an inhibitor of endosomal acidification had substantially less effect on infection mediated by the HCoV-NL63 S protein than on that mediated by the SARS-CoV S protein. Our data indicate that two coronaviruses that utilize a common receptor nonetheless enter cells through distinct mechanisms.


Subject(s)
Carboxypeptidases/metabolism , Cathepsins/physiology , Coronavirus/physiology , Cysteine Endopeptidases/physiology , Severe acute respiratory syndrome-related coronavirus/physiology , Angiotensin-Converting Enzyme 2 , Animals , Cathepsin L , Cathepsins/metabolism , Cell Line , Chlorocebus aethiops , Cysteine Endopeptidases/metabolism , Endosomes/metabolism , Green Fluorescent Proteins/metabolism , Humans , Lysosomes/enzymology , Membrane Glycoproteins/metabolism , Peptidyl-Dipeptidase A , Retroviridae/genetics , Species Specificity , Vero Cells , Viral Envelope Proteins/metabolism
7.
EMBO J ; 24(8): 1634-43, 2005 Apr 20.
Article in English | MEDLINE | ID: mdl-15791205

ABSTRACT

Human angiotensin-converting enzyme 2 (ACE2) is a functional receptor for SARS coronavirus (SARS-CoV). Here we identify the SARS-CoV spike (S)-protein-binding site on ACE2. We also compare S proteins of SARS-CoV isolated during the 2002-2003 SARS outbreak and during the much less severe 2003-2004 outbreak, and from palm civets, a possible source of SARS-CoV found in humans. All three S proteins bound to and utilized palm-civet ACE2 efficiently, but the latter two S proteins utilized human ACE2 markedly less efficiently than did the S protein obtained during the earlier human outbreak. The lower affinity of these S proteins could be complemented by altering specific residues within the S-protein-binding site of human ACE2 to those of civet ACE2, or by altering S-protein residues 479 and 487 to residues conserved during the 2002-2003 outbreak. Collectively, these data describe molecular interactions important to the adaptation of SARS-CoV to human cells, and provide insight into the severity of the 2002-2003 SARS epidemic.


Subject(s)
Carboxypeptidases/metabolism , Membrane Glycoproteins/metabolism , Severe acute respiratory syndrome-related coronavirus/metabolism , Viral Envelope Proteins/metabolism , Amino Acid Sequence , Angiotensin-Converting Enzyme 2 , Animals , Binding Sites , Carboxypeptidases/chemistry , Carboxypeptidases/genetics , Catalytic Domain , Disease Outbreaks , Humans , Models, Molecular , Molecular Sequence Data , Peptidyl-Dipeptidase A , Protein Binding , Protein Structure, Tertiary , Rats , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sequence Alignment , Severe Acute Respiratory Syndrome/epidemiology , Severe Acute Respiratory Syndrome/virology , Spike Glycoprotein, Coronavirus , Viverridae/virology
8.
Mol Microbiol ; 55(5): 1413-22, 2005 Mar.
Article in English | MEDLINE | ID: mdl-15720550

ABSTRACT

Plasmodium vivax is one of four Plasmodium species that cause human malaria. P. vivax and a related simian malaria parasite, Plasmodium knowlesi, invade erythrocytes by binding the Duffy antigen/receptor for chemokines (DARC) through their respective Duffy binding proteins. Here we show that tyrosines 30 and 41 of DARC are modified by addition of sulphate groups, and that the sulphated tyrosine 41 is essential for association of the Duffy binding proteins of P. vivax (PvDBP) and P. knowlesi (PkDaBP) with DARC-expressing cells. These sulphated tyrosines also participate in the association of DARC with each of its four known chemokine ligands. Alteration of tyrosine 41 to phenylalanine interferes with MCP-1, RANTES and MGSA association with DARC, but not with that of IL8. In contrast, alteration of tyrosine 30 to phenylalanine interferes with the association of IL8 with DARC. A soluble sulphated amino-terminal domain of DARC, but not one modified to phenylalanine at residue 41, can be used to block the association of PvDBP and PkDaBP with red blood cells, with an IC50 of approximately 5 nM. These data are consistent with a role for tyrosine sulphation in the association of many or most chemokines with their receptors, and identify a key molecular determinant of erythrocyte invasion by P. vivax.


Subject(s)
Antigens, Protozoan/metabolism , Duffy Blood-Group System/metabolism , Erythrocytes/immunology , Plasmodium vivax/metabolism , Protozoan Proteins/metabolism , Receptors, Cell Surface/metabolism , Tyrosine/metabolism , Animals , Chemokines, CXC/metabolism , Chemotactic Factors/pharmacology , Erythrocytes/parasitology , Plasmodium vivax/immunology
9.
J Virol ; 78(19): 10628-35, 2004 Oct.
Article in English | MEDLINE | ID: mdl-15367630

ABSTRACT

Infection of receptor-bearing cells by coronaviruses is mediated by their spike (S) proteins. The coronavirus (SARS-CoV) that causes severe acute respiratory syndrome (SARS) infects cells expressing the receptor angiotensin-converting enzyme 2 (ACE2). Here we show that codon optimization of the SARS-CoV S-protein gene substantially enhanced S-protein expression. We also found that two retroviruses, simian immunodeficiency virus (SIV) and murine leukemia virus, both expressing green fluorescent protein and pseudotyped with SARS-CoV S protein or S-protein variants, efficiently infected HEK293T cells stably expressing ACE2. Infection mediated by an S-protein variant whose cytoplasmic domain had been truncated and altered to include a fragment of the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein was, in both cases, substantially more efficient than that mediated by wild-type S protein. Using S-protein-pseudotyped SIV, we found that the enzymatic activity of ACE2 made no contribution to S-protein-mediated infection. Finally, we show that a soluble and catalytically inactive form of ACE2 potently blocked infection by S-protein-pseudotyped retrovirus and by SARS-CoV. These results permit studies of SARS-CoV entry inhibitors without the use of live virus and suggest a candidate therapy for SARS.


Subject(s)
Carboxypeptidases/metabolism , Leukemia Virus, Murine/physiology , Membrane Glycoproteins/genetics , Membrane Glycoproteins/metabolism , Severe acute respiratory syndrome-related coronavirus/genetics , Simian Immunodeficiency Virus/physiology , Viral Envelope Proteins/genetics , Viral Envelope Proteins/metabolism , Amino Acid Sequence , Angiotensin-Converting Enzyme 2 , Animals , Carboxypeptidases/genetics , Cell Line , HIV-1/genetics , Humans , Leukemia Virus, Murine/genetics , Leukemia Virus, Murine/metabolism , Molecular Sequence Data , Peptidyl-Dipeptidase A , Receptors, Virus/metabolism , Simian Immunodeficiency Virus/genetics , Simian Immunodeficiency Virus/metabolism , Spike Glycoprotein, Coronavirus , Virion/chemistry , Virion/metabolism , Virus Replication
10.
J Virol ; 78(20): 11429-33, 2004 Oct.
Article in English | MEDLINE | ID: mdl-15452268

ABSTRACT

Replication of viruses in species other than their natural hosts is frequently limited by entry and postentry barriers. The coronavirus that causes severe acute respiratory syndrome (SARS-CoV) utilizes the receptor angiotensin-converting enzyme 2 (ACE2) to infect cells. Here we compare human, mouse, and rat ACE2 molecules for their ability to serve as receptors for SARS-CoV. We found that, compared to human ACE2, murine ACE2 less efficiently bound the S1 domain of SARS-CoV and supported less-efficient S protein-mediated infection. Rat ACE2 was even less efficient, at near background levels for both activities. Murine 3T3 cells expressing human ACE2 supported SARS-CoV replication, whereas replication was less than 10% as efficient in the same cells expressing murine ACE2. These data imply that a mouse transgenically expressing human ACE2 may be a useful animal model of SARS.


Subject(s)
Endopeptidases/metabolism , Peptidyl-Dipeptidase A/metabolism , Severe acute respiratory syndrome-related coronavirus/physiology , Virus Replication , 3T3 Cells , Animals , Cell Line , Humans , Mice , Rats , Severe acute respiratory syndrome-related coronavirus/pathogenicity , Severe Acute Respiratory Syndrome/virology
11.
Nature ; 426(6965): 450-4, 2003 Nov 27.
Article in English | MEDLINE | ID: mdl-14647384

ABSTRACT

Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2), isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.


Subject(s)
Severe acute respiratory syndrome-related coronavirus/metabolism , Angiotensin-Converting Enzyme 2 , Animals , Antibodies/immunology , Antibodies/pharmacology , Carboxypeptidases/antagonists & inhibitors , Carboxypeptidases/genetics , Carboxypeptidases/immunology , Carboxypeptidases/metabolism , Cell Line , Chlorocebus aethiops , Giant Cells/cytology , Giant Cells/metabolism , Humans , Membrane Glycoproteins/chemistry , Membrane Glycoproteins/genetics , Membrane Glycoproteins/metabolism , Molecular Weight , Peptidyl-Dipeptidase A/immunology , Peptidyl-Dipeptidase A/metabolism , Protein Binding , Protein Structure, Tertiary , Receptors, Virus/antagonists & inhibitors , Receptors, Virus/genetics , Receptors, Virus/immunology , Receptors, Virus/metabolism , Severe acute respiratory syndrome-related coronavirus/genetics , Severe acute respiratory syndrome-related coronavirus/growth & development , Solubility , Spike Glycoprotein, Coronavirus , Transfection , Vero Cells , Viral Envelope Proteins/chemistry , Viral Envelope Proteins/genetics , Viral Envelope Proteins/metabolism , Virus Replication/drug effects
12.
Cell ; 114(2): 161-70, 2003 Jul 25.
Article in English | MEDLINE | ID: mdl-12887918

ABSTRACT

Sulfated tyrosines at the amino terminus of the principal HIV-1 coreceptor CCR5 play a critical role in its ability to bind the HIV-1 envelope glycoprotein gp120 and mediate HIV-1 infection. Here, we show that a number of human antibodies directed against gp120 are tyrosine sulfated at their antigen binding sites. Like that of CCR5, antibody association with gp120 is dependent on sulfate moieties, enhanced by CD4, and inhibited by sulfated CCR5-derived peptides. Most of these antibodies preferentially associate with gp120 molecules of CCR5-utilizing (R5) isolates and neutralize primary R5 isolates more efficiently than laboratory-adapted isolates. These studies identify a distinct subset of CD4-induced HIV-1 neutralizing antibodies that closely emulate CCR5 and demonstrate that tyrosine sulfation can contribute to the potency and diversity of the human humoral response.


Subject(s)
Antibodies, Monoclonal/metabolism , HIV Envelope Protein gp120/metabolism , HIV-1/metabolism , Receptors, CCR5/metabolism , Sulfates/metabolism , Tyrosine/metabolism , Amino Acid Sequence , B-Lymphocytes/metabolism , Binding Sites , CD4 Antigens/chemistry , CD4 Antigens/metabolism , Cell Line , Humans , Hybridomas/metabolism , Models, Biological , Molecular Sequence Data , Receptors, CCR5/chemistry , Structure-Activity Relationship
13.
J Biol Chem ; 277(43): 40397-402, 2002 Oct 25.
Article in English | MEDLINE | ID: mdl-12183462

ABSTRACT

Entry of most primary human immunodeficiency virus, type 1 (HIV-1) isolates into their target cells requires the cellular receptor CD4 and the G protein-coupled chemokine coreceptor CCR5. An acidic, tyrosine-rich, and tyrosine-sulfated domain of the CCR5 amino terminus plays a critical role in the ability of CCR5 to serve as an HIV-1 coreceptor, and tyrosine-sulfated peptides based on this region physically associate with the HIV-1 envelope glycoprotein gp120 and slow HIV-1 entry into CCR5-expressing cells. Here we show that the same tyrosine-sulfated peptides, but not their unsulfated analogs, can restore the HIV-1 coreceptor activity of a CCR5 variant lacking residues 2-17 of its amino terminus. Additionally, these sulfated peptides restored the ability of this CCR5 variant to mobilize calcium in response to the chemokines macrophage inflammatory factors 1alpha and 1beta. These observations show that a tyrosine-sulfated region of the CCR5 amino terminus can function independently to mediate association of chemokines and the HIV-1 envelope glycoprotein with the remaining domains of CCR5.


Subject(s)
Peptides/metabolism , Receptors, CCR5/metabolism , Sulfates/metabolism , Tyrosine/metabolism , Amino Acid Sequence , Calcium/metabolism , HIV-1/metabolism , Molecular Sequence Data , Receptors, CCR5/chemistry , Receptors, CCR5/genetics
14.
J Biol Chem ; 277(33): 29484-9, 2002 Aug 16.
Article in English | MEDLINE | ID: mdl-12034737

ABSTRACT

The chemokine receptor CXCR4 plays critical roles in development, immune function, and human immunodeficiency virus type 1 (HIV-1) entry. Here we demonstrate that, like the CC-chemokine receptors CCR5 and CCR2b, CXCR4 is posttranslationally modified by sulfation of its amino-terminal tyrosines. The sulfate group at tyrosine 21 contributes substantially to the ability of CXCR4 to bind its ligand, stromal derived factor 1 alpha. Tyrosine sulfation plays a less significant role in CXCR4-dependent HIV-1 entry than in CCR5-dependent HIV-1 entry. In some cell lines, CXCR4 is efficiently modified by a chondroitin sulfate chain at serine 18, but neither HIV-1 entry nor stromal derived factor 1 alpha binding was affected by loss of this glycosaminoglycan. These data demonstrate a functional role for tyrosine sulfate in the CXC-chemokine receptor family and underscore a general difference in HIV-1 utilization of CCR5 and CXCR4.


Subject(s)
Chemokines, CXC/metabolism , HIV-1/physiology , Membrane Fusion/physiology , Protein Processing, Post-Translational , Receptors, CXCR4/metabolism , Amino Acid Sequence , Animals , Cell Line , Chemokine CXCL12 , Chemokines, CXC/chemistry , Chemokines, CXC/physiology , Chondroitin Sulfates/metabolism , Dogs , Humans , Molecular Sequence Data , Receptors, CXCR4/chemistry , Receptors, CXCR4/physiology , Sequence Homology, Amino Acid , Serine/metabolism , Tyrosine/analogs & derivatives , Tyrosine/metabolism
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