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PubMed1995

Contributions of individual kringle domains toward maintenance of the chloride-induced tight conformation of human glutamic acid-1 plasminogen.

The roles of each of the three omega-amino acid-binding kringles (K) of Glu1-Pg, viz., [K1Pg], [K4Pg], and [K5Pg], in engendering the Cl(-)-induced alteration to its tight (T) conformation and in effecting the epsilon-aminocaproic acid (EACA)-mediated change to the relaxed (R) protein conformation have been investigated by mutagenesis strategies wherein the omega-amino acid ligand-binding energies in the individual kringles in recombinant (r)-Glu1-Pg were greatly reduced. This was accomplished in the most conservative manner possible by altering a critical Asp residue in each relevant kringle to Asn. The particular mutations chosen were r-[D139N]Glu1-Pg, r-[D413N]Glu1-Pg, and r-[D518N]Glu1-Pg, in which a conserved Asp residue at a homologous sequence position in each of the three kringle domains is eliminated. These changes also lead to a great reduction of the EACA-binding strength of [K1Pg], [K4Pg], and [K5Pg], respectively. The s0(20,w) of wild-type (wt) r-Glu1-Pg in the presence of levels of Cl(-)-sufficient to fully occupy its binding sites on this protein was 5.9 S, a value reduced to 4.9 S as a result of addition of saturating concentrations of EACA to the Cl-/Glu1-Pg complex. Neither Cl- nor EACA substantially altered the s0(20,w) value of 5.2 S for r-[D139N]Glu1-Pg (4.8 S) or r-[D413N]Glu1-Pg (4.5 S). On the other hand, the s0(20,w) value of 5.2 S for r-[D518N]Glu1-Pg at saturating levels of Cl- is slightly reduced to 4.8 S upon addition of binding maximal concentrations of EACA.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1981

Comparative clinical trial of epsilon amino-caproic acid and tranexamic acid in the prevention of early recurrence of subarachnoid haemorrhage.

A comparative controlled clinical trial of epsilon aminocaproic acid (EACA), 36 g/day and tranexamic acid (TEA), 6 g/day, was undertaken to assess their effectiveness in reducing early recurrence of subarachnoid haemorrhage (SAH). Of 90 patients treated with EACA recurrent haemorrhage was seen in 8% of these patients and 7% of the patients developed delayed ischaemic deficit. The total pre-operative mortality in EACA-group was 11%. Of 61 patients treated with TEA, 10% had recurrent haemorrhage and delayed ischaemic deficit occurred in 5% of the patients. The total pre-operative mortality in TEA-group was 11%. No difference was found between the effectiveness and side-effects of these drugs.

Adolescent↗
PubMed2000

Role of the N-terminal region of staphylokinase (SAK): evidence for the participation of the N-terminal region of SAK in the enzyme-substrate complex formation.

Staphylokinase (SAK) forms an inactive 1:1 complex with plasminogen (PG), which requires both the conversion of PG to plasmin (Pm) to expose an active site in PG-SAK activator complex and the amino-terminal processing of SAK to expose the positively charged (Lys-11) amino-terminus after removal of the 10 N-terminal amino acid residues from the full length protein. The mechanism by which the N-terminal segment of SAK affects its PG activation capability was investigated by generating SAK mutants, blocked in the native amino-terminal processing site of SAK, and carrying an alteration in the placement of the positively charged amino acid residue, Lys-11, and further studying their interaction with PG, Pm, miniplasmin and kringle structures. A ternary complex formation between PG-SAK PG was observed when an immobilized PG-SAK binary complex interacted with free radiolabelled PG in a sandwich binding experiment. Formation of this ternary complex was inhibited by a lysine analog, 6-aminocaproic acid (EACA), in a concentration dependent manner, suggesting the involvement of lysine binding site(s) in this process. In contrast, EACA did not significantly affect the formation of binary complex formed by native SAK or its mutant derivatives. Furthermore, the binary (activator) complex formed between PG and SAK mutant, PRM3, lacking the N-terminal lysine 11, exhibited 3-4-fold reduced binding with PG, Pm or miniplasmin substrate during ternary complex formation as compared to native SAK. Additionally, activator complex formed with PRM3 failed to activate miniplasminogen and exhibited highly diminished activation of substrate PG. Protein binding studies indicated that it has 3-5-fold reduction in ternary complex formation with miniplasmin but not with the kringle structure. In aggregate, these observations provide experimental evidence for the participation of the N-terminal region of SAK in accession and processing of substrate by the SAK-Pm activator complex to potentiate the PG activation by enhancing and/or stabilizing the interaction of free PG.

Amino Acid Sequence↗
PubMed1981

gamma-aminobutyric acid in the murine brain: mass fragmentographic assay method and post-mortem changes.

An improved mass fragmentographic assay method for the determination of gamma-aminobutyric acid (GABA) in the brain is described. Applicability of the method was examined in a study of the effect of semicarbazide on GABA levels and in a separate study to confirm post-mortem increase in GABA. The method itself is based on Cattabeni's procedure in which GABA is assayed as trimethylsilyl derivative. Three improvements were made: a) application of a more suitable mass spectrometry system for GABA determination; b) use of 6-aminocaproic acid as the internal standard; c) selection f a high intensive ion (m/z 174) for mass fragmentographic analysis. The mass spectrometer used is accurate to as little as 25 pg. GABA levels after semicarbazide treatment decreased 54.4% in rat whole brain and 44.2% in the dorsal hippocampus. Rapid post-mortem increases in GABA levels were confirmed by application of the improved assay method; decreases were most clearly observable following microwave irradiation. Post-mortem changes in GABA were observed within 3 min after death, as reported by other researchers.

Amino Acids↗
PubMed2004

Antifibrinolytic drugs for acute traumatic injury.

BACKGROUND: Uncontrolled bleeding is an important cause of death in trauma victims. Antifibrinolytic treatment has been shown to reduce blood loss following surgery and may also be effective in reducing blood loss following trauma. OBJECTIVES: To quantify the effect of antifibrinolytic drugs in reducing blood loss, transfusion requirement and mortality after acute traumatic injury. SEARCH STRATEGY: We searched the Cochrane Injuries Group's Specialised Register, the Cochrane Central Register of Controlled Trials, MEDLINE, PubMed, EMBASE, Science Citation Index, National Research Register, Zetoc, SIGLE, Global Health, LILACS, and Current Controlled Trials. SELECTION CRITERIA: We included all randomised controlled trials of antifibrinolytic agents (aprotinin, tranexamic acid [TXA] and epsilon-aminocaproic acid) following acute traumatic injury. DATA COLLECTION AND ANALYSIS: The titles and abstracts identified in the electronic searches were screened by two independent reviewers to identify studies that had the potential to meet the inclusion criteria. The full reports of all such studies were obtained. From the results of the screened electronic searches, bibliographic searches, and contacts with experts, two reviewers independently selected trials meeting the inclusion criteria, with any disagreements resolved by consensus. MAIN RESULTS: Two studies met the inclusion criteria. The study by Auer (1979), with 20 randomised patients, provided no useable outcome data. The study by McMichan (1982), with 77 randomised patients, was reported in four separate reports. Outcome data were reported for death, the proportion undergoing surgical intervention and the volume of blood transfused. Because of the small number of randomised participants, the estimates for each of these outcomes were highly imprecise. Data on the proportion undergoing re-operation and the proportion receiving blood transfusion were not reported. REVIEWERS' CONCLUSIONS: There is insufficient evidence from randomised controlled trials of antifibrinolytic agents in trauma to either support or refute a clinically important treatment effect. Further randomised controlled trials of antifibrinolytic agents in trauma are required.

Antifibrinolytic Agents↗
PubMed1984

The binding of antifibrinolytic amino acids to kringle-4-containing fragments of plasminogen.

A monoclonal antibody to human plasminogen, 10-F-1, was found to interact with the lysine-binding site (LBS) on the kringle 4 (K 4) region of the molecule. This observation has been employed to measure the binding of various antifibrinolytic amino acid analogs of epsilon-aminocaproic acid (epsilon ACA) to its site on K 4 in appropriate elastolytic-derived fragments of human plasminogen and to other species of plasminogen to which antibody 10-F-1 cross-reacts. By analysis of the concentration dependence of epsilon ACA displacement of [125I]10-F-1 from human Glu1Pg, a KD for epsilon ACA of 7.1 +/- 1.0 mM was calculated. Similar experiments with K 4-containing fragments of Glu1Pg, viz., Lys77Pg, K 4, Lys77H and Val354Pg, yielded KD values of 6.6 +/- 1.0, 7.5 +/- 1.0, 6.6 +/- 1.0, and 12.0 +/- 2.0 mM, respectively. When baboon, goat, monkey, rabbit, and sheep plasminogens were substituted for human plasminogen, the KD values calculated ranged from 2.1 to 7.1 mM. The KD values for several analogs of epsilon ACA, i.e., 4-aminobutyric acid, 5-aminopentanoic acid, 8-aminooctanoic acid, L-lysine, and trans-aminomethyl cyclohexane-1-carboxylic acid, were measured to the K 4 region of Lys77Pg. The values obtained were 11.3 +/- 1.5, 9.0 +/- 1.0, 71.0 +/- 10, 38.0 +/- 5.0, and 1.1 +/- 0.4 mM, respectively. Additionally, the KD of trans-aminomethylcyclohexane-1-carboxylic acid towards the K 4 region of Glu1Pg, Lys77Pg, and isolated K 4 was found to be 2.4 +/- 0.5, 1.1 +/- 0.3, and 2.0 +/- 0.6 mM, respectively. These studies show directly that the LBS on the K 4 domain of plasminogen represents one of its 4-5 weak binding sites and that this site can be specifically probed with the use of monoclonal antibody 10-F-1. Furthermore, it appears as though this site is conserved in several important proteolytic fragments of plasminogen, providing additional evidence that these fragments exist as independent domains in the native molecule. Finally, this weak LBS on the K 4 domain of human plasminogen is also present in other species of plasminogen.

Amino Acids↗
PubMed1997

Proton equilibria in the minor groove of DNA.

Poisson-Boltzmann calculations by Pack and co-workers suggest the presence of regions of increased hydrogen ion density in the grooves of DNA. As an experimental test of this prediction, we have attached proton-sensitive probes, with variable linker lengths, to random-sequence DNA at G sites in the minor groove. The amino groups of beta-alanine, gamma-aminobutyric acid (GABA), and epsilon-aminocaproic acid have been coupled at pH 5, via a formaldehyde link, to the exocyclic amino group of guanine, utilizing a reaction that has been extensively investigated by Hanlon and co-workers. The resulting adducts at pH 5 retained duplex B form but exhibited typical circular dichroism (CD) changes previously shown to be correlated with the presence of a net positive charge in the minor groove. Increases in the solvent pH reversed the CD spectral changes in a manner suggesting deprotonation of the carboxylic acid group of the adduct. These data were used to calculate an apparent pK(a) for the COOH. The pK(a) was increased by 2.4 units for beta-alanine, by 1.7 units for GABA, and by 1.5 units for epsilon-amino caproic acid, relative to their values in the free amino acid. This agrees well with Poisson-Boltzmann calculations and the energy minimization of the structures of the adducts that place the carboxyl groups in acidic domains whose hydrogen ion density is approximately 2 orders of magnitude greater than that of bulk solvent.

Alanine↗
PubMed1989

Plasmin-mediated fibrinolysis by variant recombinant tissue plasminogen activators.

A rapid and quantitative fibrinolytic assay has been used to measure the overall activity of a recombinant tissue plasminogen activator (rTPA) preparation for dissolution of a fibrin clot by its ability to activate [Glu1]plasminogen (containing glutamic acid at position 1) to plasmin. A standard curve constructed for wild-type two-chain rTPA that contains, from the amino terminus, the finger (F)-growth factor (E)-kringle 1 (K1)-kringle 2 (K2)-serine protease (P) domains was used to assess the overall fibrin-dissolving abilities of variant recombinant molecules. Two-chain deletion mutants lacking the E domain, the F-E domains, the F-E-K1 domains, and the K1-K2 domains yielded activities ranging from 22% to 35% of the overall activity of wild-type two-chain rTPA, suggesting that both the K2 and F domains are individually responsible for a portion of the function of the molecule. Comparison of variant molecules containing F-K1-K2-P and F-K2-K2-P domains showed that the latter variant possessed a 4-fold higher activity (1.4-fold greater than that of wild-type two-chain rTPA), indicating that, for the activity measured, the presence of K2 leads to a greater effectiveness than that of K1. A plasmin cleavage-resistant mutant (Arg-275----Ser) has been used to assess possible differences in one- and two-chain rTPA in this overall activity, the former displaying 86% of the activity of the latter, suggesting that such differences are indeed small. Finally, the proper covalent attachment of the light and heavy chains of two-chain rTPA are very important to its overall fibrinolytic activity, since replacement of Cys-264 with glycine and concomitant disruption of one of the covalent attachment sites of the two chains provides a variant of rTPA with less than 2% of the activity of the wild-type two-chain molecule. The effector molecule, epsilon-amino hexanoic acid (epsilon Ahx; epsilon-aminocaproic acid), inhibits the overall fibrinolytic effect of rTPA in this system, with an effective Ki of approximately 1.5 mM. Its efficacy, as measured by the Ki, is independent of the presence of the epsilon Ahx binding regions of plasminogen and rTPA and is similar to the efficacy obtained when urokinase was the activator in place of wild-type two-chain rTPA or when activation of plasminogen was bypassed as a result of provision of preformed plasmin to the assay. The results suggest that in the overall clot lysis system, an important epsilon Ahx binding site may exist on fibrin that inhibits its dissolution by plasmin.

Biological Assay↗
PubMed1995

The importance of the hydrophobic components of the binding energies in the interaction of omega-amino acid ligands with isolated kringle polypeptide domains of human plasminogen.

Three of the five kringle domains of human plasminogen (HPg), viz the first, fourth and fifth, exhibit significantly strong binding to omega-amino acids, such as epsilon-aminocaproic acid (EACA) and transaminomethylcyclohexane-1-carboxylic acid (AMCHA). In all cases, ligand stabilization is due to ion dipole attractions of its charged groups with polypeptide side chains, as well as hydrophobic clustering of the ligand methylene groups with appropriate hydrophobic residues within the kringle domain. In order to estimate the significance of the hydrophobic components of ligand stabilization, we have sought a more detailed description of these binding interactions. The standard thermodynamic binding parameters, delta G degrees, delta H degrees and delta S degrees, for association of EACA and AMCHA with isolated recombinant kringle regions of HPg have been determined at several temperatures to evaluate the changes in standard heat capacities (delta C degrees p) accompanying these interactions. In each case, the delta C degrees p values of binding were negative and in the range -36 to -91 cal mol -1 K -1, reflective of the importance of the hydrophobic components of the binding process and their probable effects on surrounding water structure.

Amino Acids↗
PubMedDate not supplied

[Effect of structural factors on the stability of duplexes formed by oligonucleotide conjugates with minor groove ligands].

The effect of structural factors on the stability of duplexes formed by DNA minor groove binders conjugated with oligonucleotide mono- or diphosphoramidates of the general formula Oligo-MGBm (where Oligo is an oligonucleotide; m = 1 or 2; MGB is -L(Py)2R, L(Py)4R, -L(Im)4R, or -L(Py)4NH(CH2)3CO(Py)4R; Py is a 4-aminopyrrol-2-carboxylic acid residue, L is a gamma-aminobutyric acid or an epsilon-aminocaproic acid residue, R = OEt, NH(CH2)6NEt2, or NH(CH2)6N+Me3) was studied by the method of thermal denaturation. The mode of binder interaction with minor groove depends on the conjugate structure; it may be of the parallel head to head type for bisphosphoramidates and of the antiparallel head to tail type for monophosphoramidates of a hair-pin structure. The effects of the duplexes with parallel orientation (bisphosphoramidates, MGB is L(Py)4R, m = 2) and those of the hairpin structure with the antiparallel orientation (monophosphoramidates, MGB is L(Py)4(CH2)3CO(Py)4R, m = 1) on Tm values were close. The influence of the linker (L) and substituent (R) structures upon Tm was more pronounced for monophosphoramidate (MGB is L(Py)nR, m = 1) than for bisphosphoramidate (MGB is L(Py)nR, m = 2). No more than two oligopyrrolcarboxamide residues (either in parallel or antiparallel orientations) can be incorporated into the duplex minor groove. Moreover, it was shown by the example of monophosphoramidates (Oligo-L(Py)4R and Oligo-L(Py)4NH(CH2)3CO(Py)4R) that the addition of a second ligand capable of incorporation into the minor groove increased Tm of the corresponding duplex in comparison with the duplex formed by the starting monophosphoramidate. At the same time, the introduction of the ligand incapable of incorporating decreased the Tm value. The mode of interaction of the conjugated ligand with the oligonucleotide duplex is determined by its structure. For example, dipyrrolcarboxamide containing an ethoxy group at the ligand C-end stabilizes the duplex due to the stacking interaction with the terminal A*T pair, whereas tetrapyrrolcarboxamides stabilize the duplex by incorporation into the minor groove.

Amides↗
PubMed1991

Immunochemical approach to characterize advanced glycation end products of the Maillard reaction. Evidence for the presence of a common structure.

Reaction of protein amino groups with glucose (the Maillard reaction) leads from early stage products such as Schiff base and Amadori products to advanced glycation end products (AGE), structures implicated in diabetic complications and the aging process. We have prepared the polyclonal anti-AGE antibody and the monoclonal anti-AGE antibody against AGE-bovine serum albumin and made an immunochemical approach to characterize AGE structures. Both polyclonal and monoclonal antibodies reacted with AGE-proteins such as AGE-bovine serum albumin, AGE-human serum albumin, and AGE-hemoglobin but not with unmodified counterparts. Treatments of these AGE-proteins with borohydride had no effect on the immunoreactivity. Moreover, fructosyl-epsilon-caproic acid, a synthetic Amadori compound, did not serve as an antigen, indicating that these antibodies were specific for AGE products but not for early stage products of the Maillard reaction. In addition, these antibodies were also able to recognize AGE products prepared either from alpha-tosyl-1-lysine, alpha-tosyl-1-lysine methyl ester, monoaminocarboxylic acid such as epsilon-aminocaproic acid, gamma-amino-n-butyric acid, and beta-alanine. Thus, these results strongly suggest the presence of a common structure in AGE preparations, regardless of whether AGE products are generated from proteins, amino acids, or monoaminocarboxylic acids.

Antibodies, Monoclonal↗
PubMed1978

Synthetic antigens. Rabbit antibodies against interpolymer of styrene and maleic acid (PSM).

Rabbit antibodies against interpolymer of styrene and maleic acid (PSM) are described. Rabbits immunized with PSM (mol. weight 292,000) produced precipitating and non-precipitating antibodies of IgG class. Interaction of rabbit antibodies with PSM was mainly of electrostatic character. It was found that various low molecular weight compounds resembling structural unit of the polymer inhibited reaction of PSM with antibodies. The reaction was also inhibited by picric acid and epsilon-TNP-aminocaproic acid. It suggested a multifunctional character of antibodies studied. The apparent affinity constant was 2 x 10(5) M-1 for interaction of PSM with the rabbit antibodies. Spectral studies suggested the presence of tyrosine in the combining site of anti-PSM antibodies. Specifically purified antibodies showed no restriction of heterogeneity, in comparison with rabbit IgG containing anti-PSM antibodies.

Animals↗
PubMed1993

Synthesis and characterization of fluorescent neutral lipid analogs containing N-(7-nitro-2,1,3-benzoxadiazol-4-yl)-aminohexanoic acid.

The synthesis, identification and characterization of neutral lipid analogs containing N-(7-nitro-2,1,3-benzoxadiazoi-4-yl)-aminocaproic acid are reported. The acyl-imidazole derivative of the fluorescent fatty acid was used to esterify L-alpha-glycerophosphorylcholine. Fluorescent phosphatidylcholines were converted to the corresponding diacylglycerols by phospholipase C digestion. Triacylglycerols were formed by esterification with either fluorescent fatty acid-imidazole or non-fluorescent fatty acid anhydride. The 11 compounds synthesized were identified by a combination of thin layer chromatography, liquid secondary ion mass spectrometry and enzymatic digestion. A solvent system for identifying all eleven analogs by thin layer chromatography is presented. The fluorescence characteristics of these analogs are consistent with previously observed parameters of NBD-lipid analogs, including the density-dependent quenching of analogs containing multiple NBD fluorophores. These analogs mimic native lipids, as evidenced by digestions with the enzymes, porcine pancreatic lipase, phospholipase C and phospholipase A2.

4-Chloro-7-nitrobenzofurazan↗
PubMed1998

Characterization of the interaction of bovine plasmin with Streptococcus uberis.

The binding of plasmin to Streptococcus uberis strain 0140 J was optimal in the pH range 5.0-5.5. Plasmin binding decreased exponentially with increasing NaCl concentration (0-0.8 mol l-1), reaching a minimum at NaCl concentrations exceeding 0.55 mol l-1. Neither K+, Mg2+ nor the metal chelator EDTA had any effect on the interaction. Plasmin binding was prevented, in a concentration-dependent manner, by the amino acids lysine, arginine and epsilon-aminocaproic acid. Bound plasmin was also eluted from the bacterial cell using the same amino acids. Bound plasmin was lost from the bacterium in a time- and temperature-dependent fashion, the rate of plasmin loss increased with increasing temperature over the range 4-55 degrees C, and the elution of plasmin from live and heat-killed bacteria was similar. Cell-bound plasmin was only partially inhibited by the physiological inhibitor alpha 2-antiplasmin whereas the serine protease inhibitor aprotinin, and the active site titrant p-nitrophenyl-p-guanidiniobenzoate, inhibited the activity of the cell-bound plasmin by more than 95%.

Aminocaproates↗
PubMed1976

Fibrinolytic activity in utero and bleeding complications with intrauterine contraceptive devices.

Increased menstrual loss and irregular uterine bleeding are major drawbacks to acceptibility of intrauterine contraceptive devices (IUCDs). Fibrinolytic activity around IUCDs removed from 80 women was measured by embedding the device immediately after removal in a plasminogen-rich fibrin plate. In fifteen of the women an endometrial biopsy was also taken at the time of removal of the IUCD. In women who had the IUCDs removed because of bleeding a much higher fibrinolytic activity was found than in women not complaining of excessive bleeding. The fibrinolytic activity was shown to be due to plasminogen activator and not plasmin. The findings suggest that the excessive menstrual bleeding which occurs with the IUCD may be due to enhancement of fibrinolytic activity in the endometrium which can be modified by fibrinolytic inhibitors such as epsilon aminocaproic acid.

Aminocaproic Acid↗
PubMed1989

Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy.

Photo-chemically induced dynamic nuclear polarization (photo-CIDNP) one-dimensional and two-dimensional (2D) 1H-NMR techniques have been applied to the study of the kringle 4 domain of human plasminogen both ligand-free and complexed to the antifibrinolytic drugs epsilon-aminocaproic acid and p-benzylaminesulfonic acid (BASA). A number of aromatic side-chains (His3, Trp72, Tyr41, Tyr50 and Tyr74) appear to be exposed and accessible to 3-N-carboxymethyl-lumiflavin, the photopolarizing flavin dye, both in the presence and in the absence of ligands. A lesser exposure is observed for the Trp25 and Trp62 indole groups in the presence of BASA. The spin-spin (J-coupling) and dipolar (Overhauser) connectivities in the 2D experiments afford absolute assignment of aromatic resonances for the above residues, as well as of those stemming from the Trp72 ring in the presence of BASA. Moreover, a number of H beta resonances can be identified and sorted according to specific types of amino acid residues.

Aminocaproic Acid↗
PubMed1996

Preparation of glass ionomer cement using N-acryloyl-substituted amino acid monomers--evaluation of physical properties.

OBJECTIVES: The objectives of this study were (1) to develop polyacid formulations through the incorporation of amino acid-derived monomers with carboxylic acid groups at various distances away from the polymer backbone to allow for greater flexibility, less rigid ionic cluster formation and improved solubility, and (2) to test selected physical and handling properties of experimental ionomers with a conventional glass ionomer as a control. METHODS: The polycarboxylic acids prepared and used in glass ionomer formulation in this study included N-acryloylglutamic acid (AGA) and N-acryloyl-6-aminocaproic acid (AACA)- modified acrylic acid- ++itaconic acid copolymers, where the acrylic acid:itaconic acid:amino acid monomers were combined in different proportions. The characterization and purity of the monomers were determined by FTIR and their melting points. The characterization of synthesized polymers included molecular weight and relative viscosity determinations. The compressive strengths, diametral tensile strengths, flexural strengths and fracture toughness of the experimental ionomers and a commercially available ionomer (control) were measured after storage in water, at 37 degrees C for 1 h or 7 d. The working times and setting times of the experimental ionomers were compared to the control specimens. Separate analysis of variance and Tukey's tests were used to study the statistical significance of the physical strength parameters as a function of materials and storage times. RESULTS: Significant increases (p< 0.001) in diametral tensile, compressive, flexural strengths and fracture toughness were observed in the AGA co-polymers, while significant increases were observed in diametral and flexural strengths in the AACA co-polymers compared to the control Fuji II. The working and setting times of all except one experimental ionomer studied were comparable to the controls. SIGNIFICANCE: The use of amino acid-modified acrylic monomers to produce water soluble copolymers of acrylic-itaconic acid offers a new route of discovery to produce chemical-cured glass ionomers with improved physical properties. The spacer chain length, the hydrophobicity of the chains, the molecular weight and viscosity of the polymer all played important roles in determining the physical properties of the material.

Acrylates↗