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At least 19 recordsLinked to original sources
PubMed1999

Renal handling of iodobenzoates in rats.

Renal elimination pathways of three positional isomers of iodobenzoic acid (2-iodobenzoate, 3-iodobenzoate and 4-iodobenzoate radiolabelled with 125I) were compared using the perfused rat kidney in-situ. All agents were eliminated both in a parent form (involving all renal elimination mechanisms i.e. glomerular filtration, tubular secretion, and tubular reabsorption) and also metabolized to a large extent in the kidney. After 3-iodobenzoate and 4-iodobenzoate administration, the major fractions of radioactivity found in urine were in the form of their metabolites, whereas 2-iodobenzoate was eliminated into urine mostly as the parent compound. Proportions of the individual metabolites in the urine of the perfused rat kidney were similar to those in intact rats for all agents. The results suggest that the kidney is the major organ for both the excretion and metabolism of iodobenzoates in rats. The principal renal metabolic reaction for all compounds under study was conjugation with glycine to produce the corresponding hippuric acid derivatives.

Animals↗
PubMed2005

Vibrational and microbiological study on alkaline metal picolinates and o-iodobenzoates.

FT-IR and Raman experimental data were assigned to appropriate bond vibrations and used to compare the different electronic charge distributions in the aromatic rings and carboxylic anions of various lithium, sodium, potassium, rubidium and caesium o-iodobenzoates and picolinates. Then principal component analysis (PCA) was applied in order to attempt to distinguish the biological activities of these compounds according to selected band wavenumbers. The growth of the bacteria Escherichia coli and Bacillus subtilis and the yeasts Saccharomyces cerevisiae and Hansenula anomala under optimal growth conditions were measured after 24 hours of incubation by the classical plate method. The influence of the picolinates and o-iodobenzoates on the growth of these microorganisms, again after 24 hours of incubation, was also measured and compared to the effect of sodium benzoate, which was used as a reference material. In general, the o-iodobenzoates exhibited more activity against the microorganisms than the picolinates. A statistically significant linear correlation between the spectral data and the degree of influence of a given compound on microorganism growth was established. The correlation coefficients for the o-iodobenzoates were 0.696, -0.628, 0.693 and 0.755 for E. coli, B. subtilis, H. anomala and S. cerevisiae, respectively, and for the picolinates they were 0.818, 0.826, 0.821 and 0.877 for E. coli, B. subtilis, H. anomala and S. cerevisiae, respectively. Therefore, IR spectroscopy is shown to be a rapid and reliable analytical tool for preliminary estimation of the antimicrobial properties of newly synthesized compounds, that can be applied before microbial performance tests.

Bacillus subtilis↗
PubMed2004

Application of inductively coupled plasma mass spectrometry and high-performance liquid chromatography--with parallel electrospray mass spectrometry to the investigation of the disposition and metabolic fate of 2-, 3- and 4-iodobenzoic acids in the rat.

ICP-MS, HPLC-ICP-MS and HPLC-ICP-MS/ESI-MS have been applied to determine the disposition and metabolic fate of 2-, 3- and 4-iodobenzoic acids following intraperitoneal administration at 50 mg kg(-1) to male bile duct cannulated rats. Quantitative excretion balance studies based on the determination of the total iodine content of urine and bile showed that all three iodobenzoic acids were rapidly excreted. Recoveries ranging from 95 to 105% of the administered doses were achieved within 24 h of administration. Metabolite profiles for urine and bile showed extensive metabolism with unchanged iodobenzoic acids forming a minor part of the total. A combination of alkaline hydrolysis and MS enabled the identification of the major metabolites of all three iodobenzoic acids as glycine and ester glucuronide conjugates with very little if any of the parent compounds excreted unchanged.

Animals↗
PubMedDate not supplied

Method for radioiodination of proteins using N-succinimidyl 3-hydroxy-4-iodobenzoate.

A conjugation method has been developed for the radioiodination of proteins which should be adaptable to kit formulation. m-Hydroxybenzoic acid was converted to 3-hydroxy-4-[131I]iodobenzoic acid in 65% radiochemical yield using Chloramine-T as the oxidant. This intermediate was then converted to N-succinimidyl 3-hydroxy-4-[131I]iodobenzoate ([131I]mSHIB) in 75% yield by reaction with N-hydroxysuccinimide and dicyclohexylcarbodiimide in a reaction time of only 10 min. Monoclonal antibody (mAb) 81C6 was labeled in 40-60% yield by reaction with [131I]mSHIB. Performing purifications of radioiodinated compounds using cartridges instead of HPLC did not alter conjugation efficiency, mAb immunoreactivity, or tissue distribution. Thyroid uptake of labeled mAb was low but up to 2.4 times higher than that seen when the mAb was labeled with N-succinimidyl 3-[125I]-iodobenzoate. These results suggest that [131I]mSHIB may be a useful reagent for the radioiodination of proteins, particularly in contexts when less complicated purification methods would be advantageous.

Animals↗
PubMedDate not supplied

Radioiodination of proteins using N-succinimidyl 4-hydroxy-3-iodobenzoate.

N-Succinimidyl 4-hydroxy-3-[131I]iodobenzoate ([131I]SHIB) was synthesized from 4-hydroxybenzoic acid in two steps. The overall radiochemical yield was 40-56%. A monoclonal antibody (mAb) was labeled in 10-15% yield by reaction with [131I]SHIB. The specific binding of [131I]SHIB mAb to tumor homogenates in vivo was 78 +/- 3%, compared to 84 +/- 3% for the same mAb labeled using N-succinimidyl 3-[125I]iodobenzoate ([125I]SIB). Paired-label studies in normal mice demonstrated similar tissue distributions of 131I and 125I except in thyroid. In thyroid, uptake of the two isotopes was similar on day 1; however, 131I levels increased gradually to 2-3 times those of 125I by day 6. Our results indicate that loss of label in vivo from mAbs labeled using SHIB is somewhat higher than seen with SIB but significantly lower than that observed when direct iodination methods are used.

Animals↗
PubMedDate not supplied

Catabolism of radioiodinated murine monoclonal antibody F(ab')2 fragment labeled using N-succinimidyl 3-iodobenzoate and Iodogen methods.

The F(ab')2 fragment of monoclonal antibody (MAb) Me1-14 was labeled with 125I using the Iodogen method and by reaction with N-succinimidyl 3-[125I]iodobenzoate (SIB). The labeled catabolites generated after exposure to tissue homogenates in vitro and following administration of labeled F(ab')2 into normal mice were investigated by size-exclusion HPLC, gel electrophoresis, and reverse-phase HPLC. Rapid conversion of F(ab')2 to Fab was observed with both labeling methods. With F(ab')2 labeled using the Iodogen method, the primary low molecular weight catabolites appeared to be [125I]iodide and, to a lesser extent, mono[125I]iodotyrosine. With SIB, [125I]iodide and [125I]iodobenzoic acid (IBA) as well as the glycine and lysine conjugates of IBA were all observed. Differences in low molecular weight catabolic products could explain the more rapid normal tissue clearance with MAbs and MAb fragments labeled with SIB compared with those labeled using iodogen.

Animals↗
PubMedDate not supplied

Enhanced binding and inertness to dehalogenation of alpha-melanotropic peptides labeled using N-succinimidyl 3-iodobenzoate.

Two peptides of potential utility for targeting melanoma cells, alpha-melanocyte-stimulating hormone (alpha-MSH) and its more potent analogue [Nle4,D-Phe7]-alpha-MSH, were radioiodinated in 45-65% yield using N-succinimidyl 3-[125I]iodobenzoate (SIB). To determine whether this labeling method resulted in improved in vitro and in vivo characteristics, these peptides also were labeled with 131I by direct iodination with the iodogen method. For alpha-MSH, the rapid tissue clearance of both radionuclides in mice was consistent with rapid degradation of the peptide; however, significantly lower levels of 125I were observed in thyroid and stomach, reflecting a greater inertness to deiodination. More extensive comparisons were performed with [Nle4,D-Phe7]-alpha-MSH. The in vitro binding of [Nle4,D-Phe7,Lys11-(125I)IBA]-alpha-MSH (prepared using SIB) to the murine B-16 melanoma cell line, 34.1 +/- 4.7%, was more than twice as high as that for [Tyr2(131I),Nle4,D-Phe7]-alpha-MSH (15.0 +/- 0.1%), and its KD was more than 10-fold lower than that for conventionally labeled peptide (10 +/- 5 versus 140 +/- 14 pM). The normal tissue clearance of [Nle4,D-Phe7,Lys11-(125I)IBA]-alpha-MSH in mice was faster than that of [Tyr2(131I),-Nle4,D-Phe7]-alpha-MSH. The 19-40-fold lower activity concentrations of [Nle4,D-Phe7,Lys11-(125I)IBA]-alpha-MSH in tissues accumulating free iodide (thyroid and stomach) suggest a greater inertness of this peptide to deiodination. The primary urinary catabolite of [Nle4,D-Phe7, Lys11-(125I)IBA]-alpha-MSH was the lysine conjugate of iodobenzoic acid, whereas radioiodide was the chief catabolite generated from [Tyr2(131I),Nle4,D-Phe7]-alpha-MSH. We conclude that further evaluation of [Nle4,D-Phe7,Lys11-(125I)IBA]-alpha-MSH for targeting alpha-MSH receptors is warranted and that SIB may be a useful method for the radioiodination of peptides.

Amino Acid Sequence↗
PubMed2005

On the solid state structure of 4-iodobenzoic acid.

The solid-state structure of 4-iodobenzoic acid has been confirmed by variable temperature X-ray diffraction, variable temperature solid-state NMR and differential scanning calorimetry. 4-iodobenzoic acid crystallizes in the space group P2(1)/n, and dimerizes in the solid state about a center of inversion. Using extensive X-ray crystallographic data collections, the placement of the carboxylate H atoms from the residual electron density in difference Fourier maps was determined. The position of the electron density associated with the proton is found to vary with temperature in that the population of the disordered sites changes with varying temperature. Determination of the crystal structure between the temperatures of 248 and 198 K was not possible due to a phase transition, an endothermic event occurring at 230.77 K. The phase transition is also indicated by a change in the relaxation time of the ring carbon atoms in the solid-state NMR data. Though the dominating force in the dimeric unit in the solid state is the presence of strong hydrogen bonds, there are also van der Waals forces present between the iodine atoms. In the layered structure, the iodine-iodine distance is within the van der Waals contact radii, an interaction which causes a deformation in the electron density of the iodine atoms.

Calorimetry, Differential Scanning↗
PubMed2002

Improved xenograft targeting of tumor-specific anti-epidermal growth factor receptor variant III antibody labeled using N-succinimidyl 4-guanidinomethyl-3-iodobenzoate.

Monoclonal antibodies (mAbs) such as the tumor-specific anti-epidermal growth factor receptor variant III (EGFRvIII) that are internalized and degraded after cell binding necessitate the use of radioiodination methods that minimize the loss of radioactivity from the tumor cell after intracellular processing. The purpose of the current study was to determine the suitability of N-succinimidyl 4-guanidinomethyl-3-iodobenzoate (SGMIB) for labeling this internalizing mAb. A series of paired-label biodistribution experiments were performed in athymic mice bearing subcutaneous, EGFRvIII-expressing, D-256 human glioma and U87 Delta EGFR xenografts. The tissue distribution of radioiodine activity following injection of anti-EGFRvIII mAb L8A4 labeled using N-succinimidyl 4-guanidinomethyl-3-iodobenzoate (SGMIB) were compared to those for mAb labeled using Iodogen, N-succinimidyl 3-iodo-5-pyridinecarboxylate (SIPC) as well as the Boc-protected precursor of SGMIB. Tumor uptake of radioiodine activity for mAb labeled via SGMIB was significantly higher than co-administered L8A4 radioiodinated by other methods. For example, 3 days after injection, D-256 tumor uptake of L8A4 labeled via SGMIB was 20.4 +/- 4.6% ID/g compared with 11.7 +/- 5.5% ID/g when the SIPC method was used. Thyroid uptake for L8A4 (SGMIB) was up to 36 times lower than L8A4 (Iodogen) and less than 0.35% in all experiments, indicating a low degree of deiodination in vivo. These results suggest that SGMIB may be a useful reagent for the radioiodination of this internalizing anti-EGFRvIII mAb.

Animals↗
PubMedDate not supplied

A polar substituent-containing acylation agent for the radioiodination of internalizing monoclonal antibodies: N-succinimidyl 4-guanidinomethyl-3-[131I]iodobenzoate ([131I]SGMIB).

The objective of this study was to develop an acylation agent for the radioiodination of monoclonal antibodies that would maximize retention of the label in tumor cells following receptor- or antigen-mediated internalization. The strategy taken was to add a polar substituent to the labeled aromatic ring to impede transport of labeled catabolites across lysosomal and cell membranes after antibody degradation. Preparation of unlabeled N-succinimidyl 4-guanidinomethyl-3-iodobenzoate (SGMIB) was achieved in six steps from 3-iodo-4-methylbenzoic acid. Preparation of 4-guanidinomethyl-3-[131I]iodobenzoic acid from the silicon precursor, 4-(N1,N2-bis-tert-butyloxycarbonyl)guanidinomethyl-3-trimethylsilylbenzoic acid proceeded in less than 5% radiochemical yield. A more successful approach was to prepare [131I]SGMIB directly from the tin precursor, N-succinimidyl 4-(N1,N2-bis-tert-butyloxycarbonyl)guanidinomethyl-3-trimethylstannylbenzoate, which was achieved in 60-65% radiochemical yield. A rapidly internalizing anti-epidermal growth factor receptor variant III antibody L8A4 was labeled using [131I]SGMIB in 65% conjugation efficiency and with preservation of immunoreactivity. Paired-label in vitro internalization assays demonstrated that the amount of radioactivity retained in cells after internalization for L8A4 labeled with [131I]SGMIB was 3-4-fold higher than that for L8A4 labeled with 125I using either Iodogen or [125I]SIPC. Catabolite assays documented that the increased retention of radioiodine in tumor cells for antibody labeled using [131I]SGMIB was due to positively charged, low molecular weight species. These results suggest that [131I]SGMIB warrants further evaluation as a reagent for labeling internalizing antibodies.

Acylation↗
PubMed1989

Synthesis of 125I labeled N-succinimidyl p-iodobenzoate for use in radiolabeling antibodies.

A new method is reported for the synthesis of N-succinimidyl p-([125/127I]iodobenzoate (NS-p-IB) from N-succinimidyl p-(tri-n-butylstannyl)benzoate via an iodination-destannylation reaction. The tin precursor was obtained in 70% overall yield from p-bromobenzoyl chloride after a four-step synthesis. The radiochemical yield of NS-p-[125I]IB was 75%. Conjugation of NS-p-[125I]IB to rabbit IgG or bovine serum albumin gave yields of 52 and 60% respectively. In vitro the radiolabeled proteins in serum at 37 degrees C showed less than 1% deiodination by 24 h. In vivo the stability of mouse IgG (MIgG) labeled with NS-p-[125I]IB was superior to MIgG radioiodinated in the presence of chloramine-T.

Animals↗
PubMed2005

The relationship between chemical structure and antimicrobial activity of selected nicotinates, p-iodobenzoates, picolinates and isonicotinates.

Alkaline metal, calcium and magnesium p-iodobenzoates and alkaline metal nicotinates, as well as sodium and potassium picolinic and isonicotinates were investigated by means of their antimicrobial and chemical properties. The quality estimation of the influence of metal cation coordinated to the carboxylic anion of the series of studied compounds on their antimicrobial activity as well as on the vibrational structure of whole complex in water solution was done. The changes in antimicrobial properties and in charge distribution of the complex along the position of nitrogen atom in the aromatic ring in sodium and potassium complexes were investigated. The analysis of influence of iodine substituent in para position on the change of electronic charge distribution of carboxylate anion and aromatic ring was done. The relationship between electronic properties estimated by vibrational spectroscopy and antimicrobial activity of studied complexes was investigated.

Anti-Infective Agents↗
PubMed2001

m-Iodobenzoic acid complexes with selected metals: molecular structure and antimicrobial activity.

Complexes of lithium, sodium, potassium, rubidium, cesium, magnesium, calcium, manganese, and zinc with m-iodobenzoic acid were studied. The FT-IR and FT-Raman spectra of the mentioned compounds in the solid state and water solutions were recorded and analyzed. Principal component analysis (PCA) was performed on the wavenumbers of selected bands (eight bands) occurring in the vibrational spectra. The numbers obtained as a result of this procedure characterize the electronic properties of the molecule of each complex. The antimicrobial activity of the studied compounds against selected bacteria (Escherichia coli and Bacillus subtilis) and yeast (Saccharomyces cerevisiae and Hansenula anomala) was estimated. The relationship between the chemical properties (as characterized by PCA of the IR spectra) and antimicrobial properties of the compounds was examined, and a good correlation between the two factors was found.

Anti-Bacterial Agents↗
PubMed1987

Reductive dechlorination of 2,4-dichlorobenzoate to 4-chlorobenzoate and hydrolytic dehalogenation of 4-chloro-, 4-bromo-, and 4-iodobenzoate by Alcaligenes denitrificans NTB-1.

Alcaligenes denitrificans NTB-1, previously isolated on 4-chlorobenzoate, also utilized 4-bromo-, 4-iodo-, and 2,4-dichlorobenzoate but not 4-fluorobenzoate as a sole carbon and energy source. During growth, stoichiometric amounts of halide were released. Experiments with whole cells and cell extracts revealed that 4-bromo- and 4-iodobenzoate were metabolized like 4-chlorobenzoate, involving an initial hydrolytic dehalogenation yielding 4-hydroxybenzoate, which in turn was hydroxylated to 3,4-dihydroxybenzoate. The initial step in the metabolism of 2,4-dichlorobenzoate was catalyzed by a novel type of reaction for aerobic organisms, involving inducible reductive dechlorination to 4-chlorobenzoate. Under conditions of low and controlled oxygen concentrations, A. denitrificans NTB-1 converted all 4-halobenzoates and 2,4-dichlorobenzoate almost quantitatively to 4-hydroxybenzoate.

Alcaligenes↗
PubMed1976

Sodium o-iodobenzoate and hemoglobin-oxygen affinity: in vivo effects.

Sodium o-iodobenzoate (OISB) was given intravenously to 15 dogs to test the in vivo effect of this drug on the oxyhemoglobin dissociation curve. Administration of a single dose of 500 mg/kg was followed by an average increase in P50 (PO2 at 50% oxyhemoglobin saturation) of 3.6 mmHg from 26.8 +/- 0.5 to 30.4 +/- 1.8 mmHg (corrected to pH 7.4). This elevation was sustained for 7 days. During intravenous infusions of 200 mg/kg every other day for 3 wk, there was a sustained increase in P50 of 2.6 mmHg from 27.8 +/- 1.1 to 30.4 +/- 0.9 mmHg. All dogs survived the experiment and no ill effects of the drug were noted. An increase in serum lactate and pyruvate occurred in all animals following acute or chronic exposure to the drug. There was no significant change in whole blood pH, 2,3-diphosphoglycerate concentrations, intracellular pH, or serum total phosphate. Multiple infusions of sodium cyanate (50 mg/kg per day) reduced P50 by an average of 12.2 +/- 0.3 mmHg. A subsequent single infusion of OISB (500 mg/kg) failed to increase P50. Our preliminary data indicate that pharmacological manipulation of hemoglobin O2 affinity is possible with organic compounds unrelated to erythrocyte metabolism.

Animals↗
PubMed1978

Allosteric effect of o-iodobenzoate on hemoglobin.

O-Iodobenzoate interacts non-covalently with hemoglobin and lowers the oxygen affinity of the protein. In contrast to 2,3-diphosphoglycerate or inositol hexaphosphate, its interaction does not depend upon the presence of free amino groups at the beta-chain amino terminals. Lysine beta82 is one of its oxygenation linked binding sites. As with the organic phosphates, the halogenated benzoate reacts preferentially with deoxy-hemoglobin to shift the allosteric equilibrium from R to T.

Allosteric Regulation↗
PubMed1991

Effects of sodium o-iodobenzoate on acid-base parameters and survival in dogs with hemorrhagic shock.

Sodium o-iodobenzoate (OISB) produces an increase in P50 (PO2 at 50% of oxyhemoglobin saturation) and survival when infused at the time of initiation of prolonged hemorrhagic shock in dogs. Acid-base parameters improved during treatment, and plasma lactic acid concentrations showed smaller rises than in nontreated control animals. Erythrocyte 2,3-diphosphoglycerate (2,3-DPG) rose in prolonged hemorrhagic shock in the control group and conversely decreased in OISB-treated dogs. OISB did not require red cell integrity, since its effects were still more marked in hemolyzed blood. The therapeutic benefit of OISB, appears to be related to a direct effect of the agent on the hemoglobin molecule.

2,3-Diphosphoglycerate↗