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At least 19 recordsLinked to original sources

PubMed1991

Crystal structure of cholestanyl caprylate and binary phase behavior with cholesteryl caprylate.

The crystal structure of cholestanyl n-octanoate (caprylate) (C35H62O2) is monoclinic with space group A2 and cell dimensions a = 10.103(7), b = 7.646(7), c = 87.63(7) A, beta = 90.51(6) degrees; Z = 8 [two molecules (A, B) in asymmetric unit], V = 6769 A3, Dc = 1.010 g cm-3. Integrated X-ray intensities for 3798 reflections with I greater than 2 sigma (I) were measured with a rotating anode diffractometer at room temperature. The structure was determined using direct methods. Block diagonal least squares refinement gave R = 0.111. Molecules A and B have almost fully extended conformations, but differ significantly in the rotation about the ester bond and in the C17 chains. The molecular packing in the crystal structure of cholestanyl caprylate consists of stacked bilayers each having d002 = 43.8 A in thickness and within each bilayer, cholestanols pack with cholestanols and caprylate chains pack with caprylate chains. The crystal structure is very similar to that of cholesteryl myristate but is quite different from that of cholesteryl caprylate. The phase equilibria of the cholestanyl caprylate/cholesteryl caprylate binary system have been shown to involve limited mutual solubility of the two components and to have a eutectic point at 73% cholestanyl caprylate. The cholesteric mesophase is monotropic at all compositions except for a narrow range near the eutectic point where it is enantiotropic.

Cholesterol Esters↗

PubMed1994

Bilayer packing characteristics of mixed chain phospholipid derivatives: Raman spectroscopic and differential scanning calorimetric studies of 1-stearoyl-2-capryl-sn-glycero-3-phosphocholine (C(18):C(10)PC) and 1-stearoyl-2-capryl-sn-glycero-3-phospho-N-trimethylpropanolamine (C(18):C(10)TMPC).

Raman spectroscopy and high-sensitivity differential scanning calorimetry (DSC) were used to compare the effects of headgroup conformation on the acyl chain packing arrangements in two highly asymmetric phosphatidylcholine (PC) analogues, 1-stearoyl-2-capryl-sn-glycero-3-phosphocholine (C(18):C(10)PC) and a polar headgroup derivative of C(18):C(10)PC, 1-stearoyl-2-capryl-sn-glycero-3-phospho-N-trimethylpropanolami ne (C(18):C(10)TMPC), which contains an additional methylene group within the choline moiety; namely, -P-O-(CH2)3-N(CH3)3. The C(18):C(10)TMPC headgroup exhibits an extended trans conformation which is independent of bilayer phase. A comparison of gel phase spectral order parameters of the two lipid species indicates a mixed interdigitated state characteristic of three chains per headgroup for C(18): C(10)TMPC. A more intermolecularly ordered liquid crystalline phase is observed, however, for the C(18):C(10)TMPC bilayers. The phase transition cooperative unit size estimated for the C(18):C(10)PC bilayers (approximately 140 molecules per unit) is about 7-fold greater than that for the C(18):C(10)TMPC dispersions (approximately 20 molecules per unit). We suggest that the extended headgroup for C(18):C(10)TMPC induces a slight tilt in the gel phase packing arrangements for the acyl chains, which may persist in the partially interdigitated liquid crystalline phase bilayer. Macroscopically, tighter packed multilamellar dispersions of C(18):C(10)TMPC occur for systems prepared first in the presence of a higher ionic strength medium. The stacked bilayers may then be transferred to a lower ionic strength environment without loss of their more closely packed adjacent lamellae.

Calorimetry, Differential Scanning↗

PubMed2002

Enveloped virus inactivation by caprylate: a robust alternative to solvent-detergent treatment in plasma derived intermediates.

Solvent-detergent treatment, although used routinely in plasma product processing to inactivate enveloped viruses, substantially reduces product yield from the human plasma resource. To improve yields in plasma product manufacturing, a new viral reduction process has been developed using the fatty acid caprylate. As licensure of plasma products warrants thorough evaluation of pathogen reduction capabilities, the present study examined susceptibility of enveloped viruses to inactivation by caprylate in protein solutions with varied pH and temperature. In the immunoglobin-rich solutions from Cohn Fraction II+III, human immunodeficiency virus, Type-1, bovine viral diarrhea virus (BVDV), and pseudorabies virus were inactivated by caprylate concentrations of >/=9 mM, >/=12 mM, and >/=9 mM, respectively. Compared to solvent-detergent treatment, BVDV inactivation in Fraction II+III solution was significantly faster (20-60 fold) using 16 mM caprylate. Caprylate-mediated inactivation of BVDV was not noticeably affected by temperature within the range chosen manufacturing the immunoglobulin product. In Fraction II+III solutions, IgG solubility was unaffected by </=19 mM caprylate. In albumin solution from Cohn supernatant IV-1, 40 mM caprylate rapidly inactivated BVDV, demonstrating versatility in inactivating enveloped viruses potentially present in other protein solutions. Our data show that caprylate is a robust enveloped virus inactivating agent for immunoglobulins and albumin which may potentially be utilized for other proteins; viral inactivation was not adversely affected by protein content and the buffer composition conditions evaluated. Within the parameters examined, caprylate inactivation of enveloped viruses provided comparable activity or advantages relative to the current, standard solvent-detergent treatment.

Albumins↗

PubMed2004

In vitro inactivation of Escherichia coli O157:H7 in bovine rumen fluid by caprylic acid.

The antibacterial effect of caprylic acid (35 and 50 mM) on Escherichia coli O157:H7 and total anaerobic bacteria at 39 degrees C in rumen fluid (pH 5.6 and 6.8) from 12 beef cattle was investigated. The treatments containing caprylic acid at both pHs significantly reduced (P < 0.05) the population of E. coli O157:H7 compared with that in the control samples. At pH 5.6, both levels of caprylic acid killed E. coli O157:H7 rapidly, reducing the pathogen population to undetectable levels at 1 min of incubation (a more than 6.0-log CFU/ml reduction). In buffered rumen fluid at pH 6.8, 50 mM caprylic acid reduced the E. coli O157:H7 population to undetectable levels at 1 min of incubation, whereas 35 mM caprylic acid reduced the pathogen by approximately 3.0 and 5.0 log CFU/ml at 8 and 24 h of incubation, respectively. At both pHs, caprylic acid had a significantly lesser (P < 0.05) and minimal inhibitory effect on the population of total anaerobic bacteria in rumen compared with that on E. coli O157:H7. At 24 h of incubation, caprylic acid (35 and 50 mM) reduced the population of total anaerobic bacteria by approximately 2.0 log CFU/ml at pH 5.6, whereas at pH 6.8, caprylic acid (35 mM) did not have any significant (P > 0.05) inhibitory effect on total bacterial load. Results of this study revealed that caprylic acid was effective in inactivating E. coli O157:H7 in bovine rumen fluid, thereby justifying its potential as a preslaughter dietary supplement for reducing pathogen carriage in cattle.

Animals↗

PubMed1990

Cellular mechanism of caprylic acid-induced growth hormone suppression.

To determine the dynamic secretory pattern of growth hormone (GH) in the presence of free fatty acids (FFA), we studied the effect of caprylic acid on basal and rGRF(1-29)NH2 (GRF)-induced GH secretion in acutely dispersed and perifused rat pituitary cells. At a concentration of 3.0 mmol/L, caprylic acid inhibited both basal (P less than .05) and GRF-stimulated GH secretions (P less than .01), except when the maximal (near the EC100) GRF concentration of 100 pmol/L was used. Lower concentrations of caprylic acid such as 0.3 and 1.0 mmol/L significantly inhibited, in a concentration-dependent manner, GH secretion induced by a 6.25-pmol/L GRF. However, at a GRF concentration of 25 pmol/L, this inhibitory effect was abolished. The time-course of GH response to GRF was similar in both control and caprylic acid-treated cells. To elucidate the mechanism(s) of action of the caprylic acid-induced blockade of GH secretion, in 3-day cultured rat pituitary cells, the effect of caprylic acid on basal and GRF-stimulated GH and 3',5'-cyclic adenosine monophosphate (cAMP) release. We also tested its effect on the Ca2+ ionophore, A23187-induced GH release. Caprylic acid (0.3 to 3.0 mmol/L) significantly inhibited basal GH release and GRF- or A23187-induced GH secretion. Furthermore, it decreased both basal and GRF-stimulated cAMP release (P less than .05). In addition, the effect of caprylic acid on rGRF(1-29)NH2 affinity to GRF pituitary binding sites was determined using [125I-Tyr10]hGRF(1-44)NH2 as radioligand.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed2003

Low pH, caprylate incubation as a second viral inactivation step in the manufacture of albumin. Parametric and validation studies.

Caprylate has long been used as a stabiliser for albumin solutions, as well as a precipitation agent for immunoglobulins, ceruloplasmin and more recently in removing contaminants during albumin purification. Its virucidal properties have been explored and it has been proposed that the non-ionised form of the caprylate acid disrupts the integrity of the lipid bilayer and membrane associated proteins of enveloped viruses. The studies reported here further explore the use of this fatty acid to inactivate lipid-enveloped viruses in albumin manufactured for therapeutic use. Caprylate concentrations considered above solubility limits were adopted. Acidic pH was used to maximise the percentage of non-ionised caprylate and elevated temperatures were used to enhance inactivation rates. Parameters were manipulated to determine the relationship between pH, temperature and caprylate: protein ratio. These studies demonstrated that elevated temperature and low pH were critical in achieving significant reduction in virus infectivity and that the rate and extent of inactivation was sensitive to changes in caprylate:protein ratio and to changes in pH. Final inactivation conditions of 10% w/v protein, 16 mM caprylate, pH 4.5 and 30 degrees C were chosen to minimise protein dimerisation and to achieve greater than 4 log(10)inactivation of the most resistant virus tested, bovine viral diarrhoea virus. Validation studies using both model and relevant blood borne viruses demonstrated this to be a robust and effective viral inactivation step and is complementary to the commonly used pasteurisation viral inactivation step, thus providing an additional margin of safety to this valuable therapeutic blood product.

Animals↗

PubMed2002

Caprylic acid and medium-chain triglycerides inhibit IL-8 gene transcription in Caco-2 cells: comparison with the potent histone deacetylase inhibitor trichostatin A.

1. Medium-chain triglyceride (MCT) is often administered to patients with Crohn's disease (CD) or short-bowel syndrome. However, little is known about the effects of medium-chain fatty acids (MCFAs) and MCT on intestinal inflammation. In this study we examined whether caprylic acid, one of the MCFAs, and MCT suppress IL-8 secretion by differentiated Caco-2 cells. 2. We found for the first time that caprylic acid and MCT suppress IL-8 secretion by Caco-2 cells at the transcriptional level when precultured together for 24 h. We also tried to clarify the mechanism of IL-8 gene inhibition by examining the activation of NF-kappaB and other transcription factors by electrophoretic mobility shift assay (EMSA), and found that caprylic acid did not modulate their activation. 3. The result of dual-luciferase assay using Caco-2 cells transfected with IL-8 promoter/luciferase reporter plasmid revealed that caprylic acid inhibited the activation of IL-8 promoter. 4. Similar results were observed when cells were precultured with the well-known potent histone deacetylase inhibitor trichostatin A (TSA). 5. We examined the state of H4 acetylation in IL-8 promoter using the technique known as chromatin immunoprecipitation (Chr-IP). TSA rapidly induced H4 acetylation in IL-8 promoter chromatin, whereas caprylic acid did not. These results suggest that the inhibition of IL-8 gene transcription induced by caprylic acid and TSA does not necessarily require the marked suppression of transcription factors, and the mechanism of inhibition of IL-8 gene transcription may be different between caprylic acid and TSA.

Caco-2 Cells↗

PubMed2006

Inactivation of escherichia coli O157:H7 in cattle drinking water by sodium caprylate.

Escherichia coli O157:H7 is an important foodborne pathogen. Cattle serve as one of the major reservoirs of E. coli O157:H7, excreting the pathogen in feces. Environmental persistence of E. coli O157:H7 is critical in its epidemiology on farms, and the pathogen has been isolated from cattle water troughs. Thus, there is a need for an effective method for killing E. coli O157:H7 in cattle drinking water. In this study, the efficacy of sodium caprylate for killing E. coli O157:H7 in cattle drinking water was investigated. A four-strain mixture of E. coli O157:H7 was inoculated (6.0 log CFU/ml) into 100-ml samples of well water containing 0, 75, 100, or 120 mM sodium caprylate. Water samples containing 1% (wt/vol) bovine feces or feed also were included. The samples were incubated at 21 or 8 degrees C for 21 days. Water samples were analyzed for viable E. coli O157:H7 on days 0, 1, 3, 5, and 7 and weekly thereafter. Triplicate samples of each treatment and control were included, and the study was repeated twice. The magnitude of E. coli O157:H7 inactivation in water significantly increased (P < 0.01) with increases in caprylate concentration and storage temperature. At 120 mM, sodium caprylate completely inactivated E. coli O157:H7 in all the samples after 1 to 20 days, depending on the treatments. The presence of feces or feed also had a significant effect (P < 0.01) on the antibacterial property of caprylate; the presence of feces decreased the antibacterial effect, whereas addition of feed enhanced the effect. These results indicate that sodium caprylate is effective in killing E. coli O157:H7 in cattle drinking water, but detailed cattle palatability studies of water containing caprylate are necessary.

Animals↗

PubMed1994

Caprylic acid fractionation of hyperimmune horse plasma: description of a simple procedure for antivenom production.

A simple methodology for hyperimmune horse plasma fractionation, based on caprylic acid precipitation, is described. Optimal conditions for fractionation were studied; the method gives best results when concentrated caprylic acid was added to plasma, whose pH had been adjusted to 5.8, until a final caprylic acid concentration of 5% was reached. The mixture was vigorously stirred during caprylic acid addition and then for 60 min; afterwards the mixture was filtered. Non-immunoglobulin proteins precipitated in these conditions, whereas a highly enriched immunoglobulin preparation was obtained in the filtrate, which was then dialysed to remove caprylic acid before the addition of NaCl and phenol. Thus, antivenom was produced after a single precipitation step followed by dialysis. In order to compare this methodology with that based on ammonium sulfate fractionation, a sample of hyperimmune plasma was divided into two aliquots which were fractionated in parallel by both methods. It was found that caprylic acid-fractionated antivenom was superior in terms of yield, production time, albumin/globulin ratio, turbidity, protein aggregates, electrophoretic pattern and neutralizing potency against several activities of Bothrops asper venom. Owing to its efficacy and simplicity, this method could be of great value in antivenom and antitoxin production laboratories.

Ammonium Sulfate↗

PubMedDate not supplied

Experimental induction of caprylate-dependent albumin antibodies.

To provide evidence for the immune nature of the albumin agglutination phenomenon or caprylate dependent albumin agglutinins (CDAA), rabbits were injected with native serum that had been incubated in a solution of sodium caprylate. Two of three rabbits responded with the production of CDAA, which in vitro behaved identical to human antisera. Human cells were agglutinated only when caprylate stabilized albumin was added to the cell/serum mixture or when caprylate free albumin plus sodium caprylate were used. The CDAA failed to agglutinate rabbit cells, although, both human adult and cord cells were agglutinated. These experiments indicate that the CDAA represent an immune response to native albumin that had been altered by caprylate.

Agglutination↗

PubMed1989

Purification of murine IgG monoclonal antibodies by precipitation with caprylic acid: comparison with other methods of purification.

Purification of murine IgG monoclonal antibodies from ascitic fluid by precipitation with caprylic acid was compared to that: 1) by sequential precipitation with caprylic acid and (NH4)2SO4; 2) by affinity chromatography on either antiidiotypic monoclonal antibodies or antimouse IgG xenoantibodies; and 3) by sequential (NH4)2SO4 precipitation, ion exchange chromatography and high pressure liquid chromatography (referred to as HPLC). In terms of yield of antibodies, precipitation with caprylic acid is comparable to sequential precipitation with caprylic acid and (NH4)2SO4, but superior to affinity chromatography on antibodies and to HPLC. In terms of purity of antibodies, precipitation with caprylic acid is less efficient than the other three methods. It should also be noted that precipitation with caprylic acid is associated with a reduction in the affinity of some antibodies and is not suitable to purify murine IgA and IgG3.

Animals↗

PubMed1988

Fluorescence study of the membrane-perturbing action of sodium caprylate as related to promotion of drug absorption.

The medium-chain fatty acid sodium caprylate released 6-carboxyfluorescein (CF), a model compound of water-soluble drugs, from the rat small intestinal brush border membrane (BBM) vesicles and liposomes containing CF. Caprylate caused a decrease in the fluorescence polarization of dansyl chloride, fluorescein isothiocyanate, and eosin maleimide covalently labeled to BBM. This indicates a perturbation of the BBM. However, no change in the fluorescence polarization of lipid-soluble fluorescent probes (2-(9-anthroyloxy) stearic acid, 12-(9-anthroyloxy) stearic acid, and 1,6-diphenyl-1,3,5-hexatriene) labeled to BBM was produced by caprylate. These findings indicate that caprylate can increase the permeability of the plasma membranes through the perturbation of the membranes. These actions of caprylate on membranes are considered one possible mechanism by which it promotes the absorption of water-soluble and poorly absorbed drugs.

Animals↗

PubMed1991

Inactivation of lipid-enveloped viruses in proteins by caprylate.

The use of caprylate for the inactivation of lipid-enveloped viruses in biologically active proteins both plasma derived and produced by cell culture was evaluated. Viruses consisted of herpes simplex virus type I, vesicular stomatitis virus, vaccinia virus, and Sindbis virus. Utilizing the dissociation reaction and varying the concentration of the ionized form of caprylate, a specific amount of the nonionized form of caprylate was maintained over a wide pH range. Virus-spiked protein solutions contacted with caprylate provide rapid virus inactivation under a variety of conditions while maintaining the integrity of the respective protein or activity. With the exception of coagulation factor AHF, protein and biological activity yield were essentially quantitative. Caprylate is removed after treatment by size exclusion chromatography or anion/cation exchange adsorption of the protein, followed by buffer wash.

Antiviral Agents↗

PubMed2005

Antibacterial effect of caprylic acid and monocaprylin on major bacterial mastitis pathogens.

Bovine mastitis is the most significant economic drain on the worldwide dairy industry. Concerns regarding poor cure rates, emergence of bacterial resistance, and residues in milk necessitate development of alternative therapeutic approaches to antibiotics for treatment of mastitis. A variety of free fatty acids and their monoglycerides have been reported to exert antimicrobial activity against a wide range of microorganisms. The objective of our study was to examine the efficacy of caprylic acid, a short-chain fatty acid, and its monoglyceride, monocaprylin, to inactivate common mastitis pathogens, including Streptococcus agalactiae, Streptococcus dysgalactiae, Streptococcus uberis, Staphylococcus aureus, and Escherichia coli. Milk samples containing 50 mM or 100 mM caprylic acid, and 25 mM or 50 mM monocaprylin were inoculated separately with a 3-isolate mixture of each of the 5 pathogens, and incubated at 39 degrees C. Populations of surviving bacteria were determined at 0 min, 1 min, 6 h, 12 h, and 24 h of incubation. Both caprylic acid and monocaprylin reduced all 5 pathogens by >5.0 log cfu/mL after 6 h of incubation. Among the bacterial species tested, Strep. agalactiae, Strep. dysgalactiae, and Strep. uberis were most sensitive, and E. coli was most tolerant to caprylic acid and monocaprylin. Results of this study indicate that caprylic acid and monocaprylin should be evaluated as alternatives or adjuncts to antibiotics as intra-mammary infusion to treat bovine mastitis.

Animals↗

PubMed1975

Platelet reactivity ex vivo and in vivo after acute and chronic treatment with sodium caprylate.

The effect of sodium caprylate on platelet function and other hematological parameters was studied, using rabbits as experimental animals. Intravenous administration of caprylate resulted in a pronounced, although transient, inhibition of platelet reactivity as measured by the laser technique. A single oral dose of caprylate had no effect on platelet adhesiveness. Long-term oral administration of caprylate (2 and 3 weeks) to rabbits resulted in a progressive and significant decrease in platelet adhesiveness in these animals compared to that in a control group receiving saline. However, the platelet reactivity to laser damage was not changed after administration of caprylate for 3 weeks. Other hematological parameters such as hematocrit, plasma cholesterol, triglycerides, and ketone body concentrations were not altered by the treatment.

Acetoacetates↗

PubMed1963

EFFECTS OF SODIUM CAPRYLATE ON CANDIDA ALBICANS. I. INFLUENCE OF CONCENTRATION ON ULTRASTRUCTURE.

Adams, J. N. (University of Georgia, Athens), Barbara G. Painter, and W. J. Payne. Effects of sodium caprylate on Candida albicans. I. Influence of concentration on ultrastructure. J. Bacteriol. 86:548-557. 1963.-Morphological effects of exposure to various concentrations of sodium caprylate were studied in living cells and ultrathin sections of Candida albicans. Budding was inhibited when cells were cultured in 0.0025 m sodium caprylate. Cells relieved from treatment at this concentration initiated reproductive processes at a much-stimulated rate. Momentary or 30-min exposures to 0.1 m caprylate affected cells in much the same manner as those treated at the lower concentration. Alteration of ultrastructure was brought about by treating with 0.0025 and 0.005 m concentrations prior to embedding and sectioning. Condensation of vacuolar material, change in size and number of mitochondria, loss of mitochondrial cristae, and increased electron density of the cytoplasm were observed. Cellular integrity was progressively lost as a result of treatment at levels up to 0.1 m. The highly electron-dense cytoplasm of cells cultured in media containing 0.025 m or higher inhibitor appeared to break into irregular masses, but the nucleus and vacuole sometimes could be identified. Cells treated at the 0.1 m level contained a condensed mass of opaque and unidentifiable cytoplasmic constituents within the skeletal cell wall. Cytological observations were correlated with physiological studies.

Candida↗

PubMed1963

EFFECTS OF SODIUM CAPRYLATE ON CANDIDA ALBICANS. II. INFLUENCE OF VARIOUS CONCENTRATIONS ON BIOCHEMICAL CHANGES.

Payne, W. J. (University of Georgia, Athens) and E. R. Bannister. Effects of sodium caprylate on Candida albicans. II. Influence of various concentrations on biochemical changes. J. Bacteriol. 86:558-562. 1963.-Suspending resting cells of Candida albicans in buffered solutions of 0.1 m sodium caprylate resulted in leakage of K(+), protein, ribonucleic acid (RNA), and carbohydrate (including glucose) but not of deoxyribonucleic acid (DNA) or sterol. In 0.025 m caprylate, the yeast leaked carbohydrate but not any of the other metabolites, whereas at 2.5 x 10(-3)m or in buffer alone there was no significant leakage. Inclusion of 2.5 x 10(-3)m sodium caprylate in Sabouraud dextrose broth cultures, however, suppressed growth greatly. Assays of relative protein, RNA, and DNA contents of dried cells taken from the suppressed cultures revealed changes in the rates of production of each from those of untreated cultures.

Candida↗

PubMed1976

Experimental induction of caprylate-dependent albumin antibodies.

A normal donor with the caprylate-dependent albumin agglutinins volunteered to receive 50 ml. of 25% caprylate-stabilized human albumin to determine the clinical significance of the antibodies. The donor manifested no clinical sign of a reaction. Samples of blood and urine collected before, during and after administration of albumin were subjected to extensive laboratory investigation. Biochemical, immunologic, hematologic, hemostatic and immunohematologic variables investigated showed only insignificant variations in all blood and urine samples. Results indicated that the infusion of albumin was safe, for the donor showed no sign of a hemolytic, febrile, allergic or anaphylactic transfusion reaction. However, since this is the first and only reported experiment of its kind, it is deemed advisable to exercise caution when administering albumin to patients who have caprylate-dependent albumin agglutinins until sufficient supportive data attesting to the complete safety of this procedure have accumulated.

Albumins↗