Molecular Imprinting of 3-Hydroxybenzoic Acid: Special and General Binding Sites

2003 ◽  
Vol 787 ◽  
Author(s):  
Yue Hu ◽  
Robert A. Orwoll
Keyword(s):  
Binding Sites ◽  
Association Constant ◽  
Crosslinking Agent ◽  
The Other ◽  
Hydroxybenzoic Acid ◽  
Functional Monomer ◽  
Glycol Dimethacrylate ◽  
Imprinted Polymer ◽  
Site Model ◽  
Scatchard Equation

ABSTRACTA resin, imprinted with 3-hydroxybenzoic acid (3HBA), was synthesized from acrylamide (AA, the functional monomer) and ethylene glycol dimethacrylate (EGDMA, the crosslinking agent). Batch analyses showed that the imprinted polymer has a special affinity for the meta-substituted 3HBA, but not for its para-substituted isomer (4HBA) nor for benzoic acid (BA). These results are consistent with the principle that an imprinted resin's ability to recognize is dependent on the target's size, shape, and functionality. Another resin, prepared from AA and EGDMA but in the absence of a template, had similar affinities for 3HBA, 4HBA, and BA; and thus it could not differentiate among the three. The results can be interpreted with a simple two-binding-site model with one site special for 3HBA and the other being more general with similar affinities for 3HBA, 4HBA and BA. The binding of 3HBA to the imprinted resin is characterized by an association constant and the density of each kind of site using a two-site Scatchard equation. The binding sites common to both the imprinted resin and the non-imprinted reference resin were found to have greater affinity but are less numerous than the sites unique to the imprinted resin.

Preparation of a Novel Selective Adsorbent for Detection and Measurement of Mercury (II) Ions

2013 ◽  
Vol 718-720 ◽  
pp. 645-649 ◽  
Author(s):  
Mahmoud Firouzzare
Keyword(s):  
Environmental Samples ◽  
Acidic Solution ◽  
The Other ◽  
Functional Monomer ◽  
Glycol Dimethacrylate ◽  
Imprinted Polymer ◽  
Polymeric Adsorbent ◽  
Imprinted Polymers ◽  
Selective Adsorbent ◽  
Cross Linker

In this work, a polymeric adsorbent was synthesized by the imprinting technique for the measurement of Hg (II) ion from aqueous environmental samples. For this purpose, a novel aminothiol monomer has been initially synthesized then it has been used for complexing the mercury. The synthesized complex monomer copolymerized with methacrylic acid and ethylene glycol dimethacrylate and AIBN as the functional monomer, cross-linker and initiator respectively in the presence of a binary porogen of DMSO and toluene. The imprinted polymer was made after removing the mercury (II) ion by an acidic solution of thiourea. The results of batch procedures showed that the Hg (II)-imprinted polymer has adsorption capacity of 28 mg g-1and is high selective for adsorption of Hg (II) ion in competing with the other ions such as CH3Hg (I), Zn (II) and Cd (II) and also in comparing with non-imprinted polymers.

scholarly journals Interaction Study, Synthesis and Characterization of Molecular Imprinted Polymer Using Functional Monomer Methacrylate Acid and Dimethylamylamine as Template Molecule

2018 ◽  
Vol 16 (1) ◽  
pp. 12 ◽  
Author(s):  
Saeful Amin ◽  
Sophi Damayanti ◽  
Slamet Ibrahim
Keyword(s):  
Synthesis And Characterization ◽  
Template Molecule ◽  
Functional Monomer ◽  
Molecular Imprinted Polymer ◽  
Glycol Dimethacrylate ◽  
Interaction Study ◽  
Imprinted Polymer ◽  
Infrared Spectrophotometer ◽  
Scanning Electron

The research related to the interaction study, synthesis and characterization of molecular imprinted polymer using dimethylamylamine (DMAA) as the template molecule and the functional monomer methacrylate acid has been conducted. Molecular Imprinted Polymer (MIP) is a separation method made by the molecule template in the polymer matrix followed by removing the template molecule by washing for giving the permanent framework groove. The MIP was made by mixing the DMAA as the template molecule, with the methacrylate acid as the functional monomer, and the ethylene glycol dimethacrylate (EGDMA) as the crosslinker with the ratio 1:6:20. Porogen solvents used were the chloroform and the initiator azobisisobutyronitrile (AIBN). The crystal MIP and the NIP without the DMAA were characterized using Infrared Spectrophotometer (FTIR), and the result showed that there have been differences among the MIP, the NIP and the MIP after being extracted. The characterization using Scanning Electron Microscope (SEM) showed that the NIP as the comparison having flat morphology, while the MIP having irregular morphology and less pores. Then the MIP after being extracted has irregular, rough morphology and a lot of pores. The result reveals the interaction between the DMAA and the methacrylate acid that is the hydrogen bonded with the Gibbs free energy obtained is -5.434 j/mol. The imprinting factor of 2,353 is obtained. The highest desorption descending capacity is chloroform with the MIP 738% better. For the MIP and NIP methanol, it is found that the MIP is 123% better. Then the MIP which is desorbed by the chloroform is better 602% than the MIP resorbed by the methanol, and the ethyl acetate cannot desorb the DMAA.

scholarly journals Synthesis and Characterization of a Molecularly Imprinted Polymer of Spermidine and the Exploration of Its Molecular Recognition Properties

Polymers ◽  
2018 ◽  
Vol 10 (12) ◽  
pp. 1389 ◽  
Author(s):  
Yu-Jie Huang ◽  
Rui Chang ◽  
Qiu-Jin Zhu
Keyword(s):  
Molar Ratio ◽  
Template Molecule ◽  
Functional Monomer ◽  
Imprinted Polymer ◽  
Polymer Complexes ◽  
Molecular Imprinting Technology ◽  
Recognition Ability ◽  
Scatchard Equation ◽  
Factor Α

Spermidine is a functional ingredient that can extend the lifespan of many foods and indicate meat safety. However, its synthesis and enrichment is expensive and complex. To develop an effective separation material that can offer highly selective recognition of spermidine, we first applied non-covalent molecular imprinting technology using methacrylic acid as a functional monomer, azobisisobutyronitrile as an initiator, and ethylene glycol dimethacrylate as a cross-linker. The adsorption properties of the polymers were analyzed using the Scatchard equation, the Lagergren kinetic equation, and the static distribution coefficient. The optimal polymerization molar ratio of the template molecule spermidine to the functional monomer was 1:4, the maximum adsorption amount was 97.75 μmol/g, and the adsorption equilibrium time was 300 min. The selective experiment showed that the interfering substances tyramine and histamine had selectivity factor α values of 2.01 and 1.78, respectively, indicating that the prepared polymer had good spermidine recognition ability. The density function theory calculations showed that the hydrogen bond strength, steric effect, and product energy caused adsorption and separation differences among the different imprinted polymer complexes.

scholarly journals Investigation of the mechanism by which glucose analogues cause translocation of glucokinase in hepatocytes: evidence for two glucose binding sites

2000 ◽  
Vol 346 (2) ◽  
pp. 413-421 ◽  
Author(s):  
Loranne AGIUS ◽  
Mark STUBBS
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
The Other ◽  
Hill Coefficient ◽  
Site Model ◽  
Glucose Binding ◽  
Glucose Analogues ◽  
Hill Coefficients ◽  
Effect Of Glucose ◽  
Kinetics Of

Glucokinase translocates between the cytoplasm and nucleus of hepatocytes where it is bound to a 68 kDa protein. The mechanism by which glucose induces translocation of glucokinase from the nucleus was investigated using glucose analogues that are not phosphorylated by glucokinase. There was strong synergism on glucokinase translocation between effects of glucose analogues (glucosamine, 5-thioglucose, mannoheptulose) and sorbitol, a precursor of fructose 1-phosphate. In the absence of glucose or glucose analogues, sorbitol had a smaller effect than glucose on translocation. However, sorbitol potentiated the effects of glucose analogues. In the absence of sorbitol the effect of glucose on glucokinase translocation is sigmoidal with a Hill coefficient of 1.9 suggesting involvement of two glucose-binding sites. The effects of glucosamine and 5-thioglucose were also sigmoidal but with lower Hill Coefficients. In the presence of sorbitol, the effects of glucose, glucosamine and 5-thioglucose were hyperbolic. Mannoheptulose, unlike the other glucose analogues, had a hyperbolic effect on glucokinase translocation in the absence of sorbitol suggesting interaction with one site and was synergistic rather than competitive with glucose. The results favour a two-site model for glucokinase translocation involving either two glucose-binding sites or one binding-site for glucose and one for fructose 1-phosphate. The glucose analogues differed in their effects on the kinetics of purified glucokinase. Mannoheptulose caused the greatest decrease in co-operativity of glucokinase for glucose whereas N-acetylglucosamine had the smallest effect. The anomalous effects of mannoheptulose on glucokinase translocation and on the kinetics of purified glucokinase could be explained by a second glucose-binding site on glucokinase.

Binding Studies on Resins Imprinted with (S)-naproxen

2002 ◽  
Vol 723 ◽  
Author(s):  
Yue Hu ◽  
Robert A. Orwoll
Keyword(s):  
Free Radical ◽  
Binding Sites ◽  
Affinity Binding ◽  
Binding Parameters ◽  
Glycol Dimethacrylate ◽  
Binding Studies ◽  
Number Of Binding Sites ◽  
Scatchard Equation ◽  
Non Covalent Interactions ◽  
Covalent Interactions

AbstractResins were prepared in a free-radical polymerization of 4-vinylpyridine and ethylene glycol dimethacrylate in the presence of (S)-(+)-6-methoxy-α-methyl-2-naphtaleneacetic acid ((S)-naproxen). Initially (S)-naproxen, the imprinted molecule template, was assembled with the monomer 4-vinylpyridine by non-covalent interactions. After the polymerization, stepwise removal of the template left binding sites that retain complementary specificity and affinity. Binding parameters including the maximum number of binding sites and dissociation constant were calculated from the amount of template removed using a two-site Scatchard equation. The results are typical of other systems reported in the literature.

THE MOLECULAR ORGANIZATION OF HUMAN ALPHA 2-MACROGLOBULIN. AN IMMUNO ELECTRON MICROSCOPIC STUDY WITH MONOCLONAL ANTIBODIES

1987 ◽  
Author(s):  
E Delain ◽  
M Barrav ◽  
J Tapon-Bretaudière ◽  
F Pochon ◽  
F Van Leuven
Keyword(s):  
Monoclonal Antibodies ◽  
Binding Sites ◽  
Divalent Cations ◽  
The Other ◽  
Molecular Organization ◽  
Cellular Receptor ◽  
Electron Microscopic ◽  
Microscopic Method ◽  
Bait Region ◽  
Electron Microscopic Method

Electron microscopy is a very convenient method to localize the epitopes of monoclonal antibodies (mAbs) at the surface of macromolecules for studying their tree-dimensional organization.We applied this immuno-electron microscopic method to human ct2-macroglobulin (ct2M). 29 anti-α2M mAbs have been tested with the four different forms of a2M : native and chymotrypsin-transformed tetramers, and the corresponding dimers, obtained by dissociation with divalent cations. These mAbs can be classified in three types : those which are specific for 1) the H-like transformed molecules, 2) the native molecules, and 3) those which can react with both forms of α2M.1) Among the H-like α2M specific mAbs, several react with the 20 kD-domain which is recognized by the cellular receptor of transformed a2M. This domain is located at the carboxyterminal end of each monomer. One IgG binds to the end of two adjacent tips of the H-like form.The other mAbs of this type bind to the α2M tips at non-terminal positions. Intermolecular connections built polymers of alternating α2M and IgG molecules.2) Among the native a2M-specific mAbs some are able to inhibit the protease-induced transformation of the native α2M. The binding sites of these mAbs are demonstrated on the native half-molecules. One of these mAbs was also able to react with transformed dimers, in a region corresponding very likely to an inaccessible epitope in the tetrameric transformed α2M molecule.3) Among the mAbs of this type, only two were able to inhibit the protease-induced transformation of α2M. Obviously, their epitopes should be close to the bait region of α2M. The other mAbs reacting with both α2M forms did not inhibit the α2M transformation.All these mAbs can be distinguished by the structure of the immune complexes formed with all forms of α2M. The epitopes are more easily located on the dimers and on the H-like transformed α2M than on the native molecules.From these observations, we propose a new model of the tree-dimensional organization of the human α2M in its native and transformed configurations, and of its protease-induced transformation.

Gold (Au) selective adsorption using polyeugenol based ionic imprinted polymer with ethylene glycol dimethacrylate crosslink

2020 ◽  
Author(s):  
M. Cholid Djunaidi ◽  
Nor Basid Adiwibawa Prasetya ◽  
Didik Setiyo Widodo ◽  
Retno Ariadi Lusiana ◽  
Pardoyo
Keyword(s):  
Ethylene Glycol ◽  
Selective Adsorption ◽  
Ethylene Glycol Dimethacrylate ◽  
Glycol Dimethacrylate ◽  
Imprinted Polymer

scholarly journals Novel Interactions of ESCRT-III with LIP5 and VPS4 and their Implications for ESCRT-III Disassembly

2008 ◽  
Vol 19 (6) ◽  
pp. 2661-2672 ◽  
Author(s):  
Soomin Shim ◽  
Samuel A. Merrill ◽  
Phyllis I. Hanson
Keyword(s):  
Atpase Activity ◽  
Binding Site ◽  
Binding Sites ◽  
Essential Role ◽  
Multivesicular Body ◽  
The Other ◽  
Aaa Atpase ◽  
Direct Binding ◽  
Novel Interactions

The AAA+ ATPase VPS4 plays an essential role in multivesicular body biogenesis and is thought to act by disassembling ESCRT-III complexes. VPS4 oligomerization and ATPase activity are promoted by binding to LIP5. LIP5 also binds to the ESCRT-III like protein CHMP5/hVps60, but how this affects its function remains unclear. Here we confirm that LIP5 binds tightly to CHMP5, but also find that it binds well to additional ESCRT-III proteins including CHMP1B, CHMP2A/hVps2–1, and CHMP3/hVps24 but not CHMP4A/hSnf7–1 or CHMP6/hVps20. LIP5 binds to a different region within CHMP5 than within the other ESCRT-III proteins. In CHMP1B and CHMP2A, its binding site encompasses sequences at the proteins' extreme C-termini that overlap with “MIT interacting motifs” (MIMs) known to bind to VPS4. We find unexpected evidence of a second conserved binding site for VPS4 in CHMP2A and CHMP1B, suggesting that LIP5 and VPS4 may bind simultaneously to these proteins despite the overlap in their primary binding sites. Finally, LIP5 binds preferentially to soluble CHMP5 but instead to polymerized CHMP2A, suggesting that the newly defined interactions between LIP5 and ESCRT-III proteins may be regulated by ESCRT-III conformation. These studies point to a role for direct binding between LIP5 and ESCRT-III proteins that is likely to complement LIP5's previously described ability to regulate VPS4 activity.

Cell adhesion and phagocytosis promoted by monoclonal antibodies not directed against fibronectin receptors

1988 ◽  
Vol 90 (2) ◽  
pp. 201-214 ◽  
Author(s):  
F. Grinnell ◽  
C.H. Ho ◽  
T.L. Tuan
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Adhesion ◽  
Binding Sites ◽  
Cell Spreading ◽  
The Other ◽  
Immunofluorescence Staining ◽  
Baby Hamster Kidney ◽  
Bhk Cells ◽  
Reducing Conditions ◽  
Latex Beads

In this report we describe cell adhesion and phagocytosis promoted by two monoclonal antibodies that were selected for immunofluorescence staining of non-permeabilized baby hamster kidney (BHK) cells. Anti-BHK1 staining was heaviest along cell margins, whereas anti-BHK2 staining was continuous along cell margins. Neither antibody stained elongated plaque structures such as were observed when cells were reacted with antibodies to fibronectin (FN) receptors. The monoclonal antibodies functioned as adhesion ligands in four different assays: attachment to culture dishes, spreading, binding of latex beads and phagocytosis. Anti-BHK1 and anti-BHK2 promoted attachment to culture dishes similarly, but anti-BHK2 was more effective at promoting cell spreading. Antibody-promoted cell spreading was inhibited by the peptides Ser-Asp-Gly-Arg and Gly-Arg-Gly-Asp-Ser-Pro but not by other, related, peptides tested. The monoclonal antibodies also promoted binding of latex beads, and the bead binding sites were motile, on the basis of their ‘capping’ response. Nevertheless, anti-BHK2 beads were phagocytosed by cells 5- to 20-fold more efficiently than anti-BHK1 beads. The binding sites for anti-BHK1 and anti-BHK2 were characterized by immunoprecipitation experiments. Anti-BHK1 binding sites contained 50K (K = 10(3) Mr) and 88K components under non-reducing conditions that migrated as a 51/53K doublet and a 93K component under reducing conditions. On the other hand, anti-BHK2 binding sites contained 88K and 110K components under non-reducing conditions that shifted to apparent 107K and 128K values when measured under reducing conditions.

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