Arginine Solution Research Articles

Isomerization of aldo-disaccharides to keto-disaccharides in arginine solution and phosphate buffer under subcritical conditions

Maltose, cellobiose, and lactose dissolved in 0.01 mol/L arginine solution or 0.01 mol/L phosphate buffer (pH 7.0) at 0.2 mol/L were reacted batchwise at 110 °C. The yields of the corresponding keto-disaccharides were 23.4% and 17.6% for maltose, 19.3% and 13.0% for cellobiose, and 20.0% and 13.7% for lactose in arginine solution at 30 min and phosphate buffer at 150 min, respectively. All the disaccharides were hydrolyzed in the range of 0.5 to 3.5%, the degree of hydrolysis being greater in arginine solution than in phosphate buffer. The monosaccharides produced by hydrolysis were slightly isomerized to other monosaccharides. A decrease in pH and an increase in absorbance at 280 and 420 nm continued even at the almost constant yields of the main products. The browning was particularly pronounced in the latter half of the reaction, suggesting a change of the by-products to substances with high absorption coefficient.

Arginine: a useful treatment to delay enzymatic browning of fresh-cut pear and apple

This study examined the effect of arginine treatments on the prevention of enzymatic browning in fresh-cut apples and pears. For this, 0, 25, 50, 75, and 100 mM, and 0-, 50-, 100-, and 200-mM arginine solutions were prepared for apples and pears, respectively. Slices of both fruits were dipped in these solutions for 5 min and dried for 20 min. Then, they were packaged and stored at 5±1oC temperature and 80-90% relative humidity for 18 days for pears and 12 days for apples. Browning index, color values, weight losses, firmness of slices, and total soluble solids were examined at three-day intervals during storage. The results showed that arginine treatment retarded the enzymatic browning of both apple and pear slices. While arginine suppressed browning at increasing doses, especially at 200 mM in pears, it retarded browning in apple slices at all concentrations. In addition, the fact that the L values were higher than the control and water control applications showed that both apple and pear slices remained lighter in color. Hue values supported both the L and browning index results. Arginine treatment decreased the weight loss; however, it did not affect the firmness of the slices. In addition, arginine treatments did not have a significant effect on the total soluble solid content of apple and pear slices.

Chemical Characterization of the Precipitate Found in and Its Effect on Drug Release of the Scutellaria baicalensis-Coptis chinensis Extract.

Precipitate generation is a challenging issue during the production of herbal decoction as it affects the stability and bioavailability of active compounds. Here we explored the composition of the natural precipitate formed from and its effect on drug release of Scutellaria baicalensis-Coptis chinensis paired extract (SCPE). Furthermore, the surface morphology of the SCPE precipitate was also investigated. Ultra-performance liquid chromatography-mass spectrometry (UPLC-MS) was used to chemical component analysis and field emission scanning electron microscope (FE-SEM) was performed to particle observation. Baicalin (BA), berberine (BBR) and starch-arginine-rich polymers were abundant in the SCPE precipitate. FE-SEM micrographs showed spheroidal shaped particles in the SCPE supernatant, while spherical and porous tissue-shaped particles in the SCPE precipitate. In vitro drug release of baicalin and berberine contained in the precipitate may increase as the polymer is removed. The presence of polymer-related interactions were confirmed by the greater increase in solubility of baicalin upon addition of arginine and polymer. This was also supported by the solubility decrease of the BA-BBR complex in polymer solution and the gelation of the BA-BBR complex in arginine solution. Our results provide a scientific basis for elucidating the pharmaceutical properties of the decoction of S. baicalensis-C. chinensis-based herbal medicine.

LC-MS/MS Analysis of Reaction Products of Arginine/Methylarginines with Methylglyoxal/Glyoxal.

Methylglyoxal (MGO) and glyoxal (GO) are toxic α-dicarbonyl compounds that undergo reactions with amine containing molecules such as proteins and amino acids and result in the formation of advanced glycation end products (AGEs). This study aimed at investigating the reactivity of arginine (Arg) or dimethylarginine (SDMA or ADMA) with MGO or GO. The solutions of arginine and MGO or GO were prepared in PBS buffer (pH 7.4) and incubated at 37 °C. Direct electrospray ionization-high-resolution mass spectrometry (ESI-HRMS) analysis of the reaction mixture of Arg and MGO revealed the formation of Arg-MGO (1:1) and Arg-2MGO (1:2) products and their corresponding dehydrated products. Further liquid chromatography (LC)-MS analyses revealed the presence of isomeric products in each 1:1 and 1:2 product. The [M + H]+ of each isomeric product was subjected to MS/MS experiments for structural elucidation. The MS/MS spectra of some of the products showed a distinct structure indicative fragment ions, while others showed similar data. The types of products formed by the arginines with GO were also found to be similar to that of MGO. The importance of the guanidine group in the formation of the AGEs was reflected in similar incubation experiments with ADMA and SDMA. The structures of the products were proposed based on the comparison of the retention times and HRMS and MS/MS data interpretation, and some of them were confirmed by drawing analogy to the data reported in the literature.

Isomerization and epimerization of glucose and galactose in arginine solution and phosphate buffer under subcritical fluid conditions.

Reaction of glucose or galactose was performed in arginine solution or phosphate buffer (pH 7.0) using a batch reactor at 110°C. The yields of products, pH, and absorbances at 280 and 420nm were measured during the reaction. Fructose, mannose, and allulose were formed from glucose; tagatose, talose, and sorbose were done from galactose. The reaction proceeded more rapidly in arginine solution than in phosphate buffer. In arginine solution, yields of fructose and tagatose were 20% and 16%, respectively, after 30-min reaction; in phosphate buffer, they were 14% and 10%, respectively. However, in both reaction media, the pH drop and increase in absorbances continued even after the yield became almost constant. The absorbance increased particularly in the latter half of the reaction due to formation of browning products. Therefore, to avoid browning, the reaction should be stopped as soon as possible after the yield approaches its maximum value.

Isomerization of pentoses in arginine solution and phosphate buffer at 110 °C

Ribose, xylose, or arabinose at 0.2 mol/L was dissolved in 0.01 mol/L arginine or 0.01 mol/L phosphate buffer (pH 7.0) and treated at 110 °C. The yield of ribulose, xylulose, and ribulose, the pH, and the absorbance at 280 and 420 nm of the reaction mixture were measured. The reaction proceeded rapidly in highly alkaline arginine solution, and the apparent equilibrium yields of ribulose, xylulose, and ribulose were 8.8, 8.9, and 3.5%, respectively. In phosphate buffer, the yields of ribulose, xylulose, and ribulose were 8.4, 6.5, and 2.2%, respectively. In both cases, even after the yields became almost constant, the decrease in pH and the increase in absorbance at 280 and 420 nm continued. The increase in absorbance was particularly remarkable in the latter half of the reaction. Therefore, it is preferable to stop the reaction as soon as possible when the yield of the product reached the maximum value.

Preparation and evaluation of a novel alginate-arginine-zinc ion hydrogel film for skin wound healing

In this paper, the mixed solution of sodium alginate (SA) and arginine (Arg) was dried into a film and then crosslinked with zinc ion to form sodium alginate-arginine-zinc ion (SA-Arg-Zn2+) hydrogel for skin wound dressings. SA-Arg-Zn2+ hydrogel had higher swelling ability, which was beneficial to absorbing wound exudate. Moreover, it exhibited antioxidant activity and strong inhibition against E. coli and S. aureus, and had no obvious cytotoxicity to NIH 3T3 fibroblasts. Compared with other dressings utilized in rat skin wound, SA-Arg-Zn2+ hydrogel showed better wound healing efficacy and the wound closure ratio reached to 100 % on the 14th day. The result of Elisa test indicated that SA-Arg-Zn2+ hydrogel down-regulated the expression of inflammatory factors (TNF-α and IL-6) and promoted the growth factor levels (VEGF and TGF-β1). Furthermore, H&E staining results confirmed that SA-Arg-Zn2+ hydrogel could reduce wound inflammation and accelerate re-epithelialization, angiogenesis and wound healing. Therefore, SA-Arg-Zn2+ hydrogel is an effective and innovative wound dressing, moreover, the preparation technique is simple and feasible for industrial application.

Antimicrobial Activity and Cytotoxicity of Nonsteroidal Anti-Inflammatory Drugs against Endodontic Biofilms.

Persistent infections have become a challenge in dentistry because of growing antibiotic resistance. Nonsteroidal anti-inflammatory drugs (NSAIDs) appear to be a therapeutic alternative to control biofilm infection. The objective of this work is to evaluate the antimicrobial activity and cytotoxicity of sodium diclofenac (DCS), ibuprofen (IBP) and ibuprofen arginine (IBP-arginine) solutions against endodontic polymicrobial biofilms. Sterile radicular dentin blocks of 4 mm × 4 mm × 0.7 mm were used as substrate to grow biofilm. The dentin blocks were submerged into solutions for 5 min. The antimicrobial activity was evaluated by means of the adenosine triphosphate (ATP) assay and confocal laser scanning microscopy (CLSM). Fibroblasts 3T3-L1 (ECACC 86052701) were used to test the cytotoxicity of irrigating solutions. The antibiofilm effects determined by the ATP assay showed that 4% IBP-arginine solution exerted the highest antibiofilm activity, followed by 4% DCS and 4% IBP, with statistical differences among groups (p < 0.001). As for CLSM, 4% DCS and 4% IBP-arginine solutions gave the lowest viable cell percentages, without significant differences between them. Cytotoxicity results at 1/10 dilution were similar for all solutions. At 1/100 dilution, a 4% DCS solution obtained the lowest cell viability for both time periods assayed, 1 h and 24 h. The IBP-arginine group showed the highest cell viability at 24 h. In this preliminary study, in terms of antibiofilm activity and cytotoxicity, a mixed 4% IBP-arginine solution gave the most promising results. NSAID solutions could be recommendable drugs for endodontic disinfection procedures.

Effect of Functionalization of the Polycaprolactone Film Surface on the Mechanical and Biological Properties of the Film Itself.

The lack of suitable functional groups for cell adhesion on the surface of Polycaprolactone (PCL) is one of the main limitations in order to use PCL for biomedical applications. The aim of this research is to modify the PCL film surface using arginine, via an aminolysis reaction. In this regard, after PCL films formation by casting method, they were immersed in arginine solutions of various concentration at room temperature or then heated to 40 °C and in the presence of isopropanol or without it. To assess the structure of the modified surface, its wettability, and mechanical properties, methods of measuring the contact angle and the strip tensile test were used, and to compare the degree of attachment and the rate of cell proliferation, the method of fluorescent staining of cultured cells was used. The change in protein synthesis by cells on the modified surface was assessed using Western blotting. The results obtained show that the treatment of PCL films with an aqueous solution of arginine at room temperature for 1 day increases the hydrophilicity of the surface. Wherein surface modification led to a two-fold decrease of mechanical strength and flow stress, but elongation increase by about 30% for PCL films after modification in 0.5 M aqueous arginine solution at room temperature. Moreover, cell attachment and proliferation, as well as collagen synthesis, were significantly enhanced after arginine modification. The proposed simple and effective method for modifying PCL films with arginine significantly expands the possibilities for developing biocompatible scaffolds for tissue engineering.

Ion mobility mass spectrometry with surface activated chemical ionisation as a method for studying the domain of water clusters.

Water holds great relevance in various biological and biochemical systems. Water behaves as an excellent solvent, a reactant, a product and a catalyst of the reaction. The organisation of the water molecules, synergised by hydrogen bonds, builds up the structure of the water clusters. These water clusters significantly influence biological functions. To study the domain of water clusters using Ion mobility mass spectrometry with surface activated chemical ionisation. The experimental analysis was aimed to determine the water behaviour in terms of cluster formation before and after the application of a physical effect, namely low-frequency irradiation. A sanist platform-based spectrometer, manufactured by ISB srl with SACI version for protein analysis, was used as the equipment. Furthermore, for samples, we used pure de-ionised water, a part of which was used virgin, and another part was irradiated. Ion-mobility mass spectrometry (IM-MS) procedure was adopted as the experimental method. An electromagnetic frequency fields generator was used to subject the test samples to electromagnetic radiations between 7 Hz to 80 Hz. The presence of neutral water species was confirmed in the water samples. For the same m/z, water ion clusters in the untreated water were found to have a much higher intensity than the electromagnetically treated water. The presence of a water cluster near the (M+H)+ in electromagnetically treated dilute arginine solution was also confirmed. It is possible to detect water ion clusters by using Ion mobility mass spectrometry and SACI with low surface potential (47 V). The water cluster formation and its characteristics were found to be different in the treated and non-treated water. The electromagnetic radiations of low frequency seem to affect the hydrogen bonds of the water molecules.

Role of arginine salts in preventing freezing-induced increase in subvisible particles in protein formulations

While arginine hydrochloride (ArgHCl) has emerged as a potential stabilizer of protein drugs in liquid formulations, the purpose of this manuscript was to evaluate its stabilization potential in frozen solutions. The phase behavior of frozen ArgHCl solutions was investigated by differential scanning calorimetry and low temperature powder X-ray diffractometry. The aggregation of β-galactosidase was evaluated following freeze–thaw cycling in ArgHCl solutions with and without mannitol. ArgHCl (5% w/v) was retained amorphous in frozen aqueous solutions and effectively inhibited protein aggregation even after 5 freeze–thaw cycles. Annealing frozen arginine solution (5% w/v) containing mannitol (10% w/v) induced mannitol crystallization which in turn facilitated crystallization of ArgHCl. The stabilizing effect of ArgHCl was completely lost in the presence of mannitol. Use of alternate arginine salts (aspartate, glutamate, and acetate) allowed selective crystallization of mannitol while arginine was retained amorphous and stabilized the protein.

Influence of Aqueous Arginine Solution on Regulating Conformational Stability and Hydration Properties of the Secondary Structural Segments of a Protein at Elevated Temperatures: A Molecular Dynamics Study.

The effects of aqueous arginine solution on the conformational stability of the secondary structural segments of a globular protein, ubiquitin, and the structure and dynamics of the surrounding water and arginine were examined by performing atomistic molecular dynamics (MD) simulations. Attempts have been made to identify the osmolytic efficacy of arginine solution, and its influence in guiding the hydration properties of the protein at an elevated temperature of 450 K. The similar properties of the protein in pure water at elevated temperatures were computed and compared. Replica exchange MD simulation was performed to explore the arginine solution's sensitivity in stabilizing the protein conformations for a wide range of temperatures (300-450 K). It was observed that although all the helices and strands of the protein undergo unfolding at elevated temperature in pure water, they exhibited native-like conformational dynamics in the presence of arginine at both ambient and elevated temperatures. We find that the higher free energy barrier between the folded native and unfolded states of the protein primarily arises from the structural transformation of α-helix, relative to the strands. Our study revealed that the water structure around the secondary segments depends on the nature of amino acid compositions of the helices and strands. The reorientation of water dipoles around the helices and strands was found hindered due to the presence of arginine in the solution; such hindrance reduces the possibility of exchange of hydrogen bonds that formed between the secondary segments of protein and water (PW), and as a result, PW hydrogen bonds take longer time to relax than in pure water. On the other hand, the origin of slow relaxation of protein-arginine (PA) hydrogen bonds was identified to be due to the presence of different types of protein-bound arginine molecules, where arginine interacts with the secondary structural segments of the protein through multiple/bifurcated hydrogen bonds. These protein-bound arginine formed different kinds of bridged PA hydrogen bonds between amino acid residues of the same secondary segments or among multiple bonds and helped protein to conserve its native folded form firmly.

Корекція ендотеліальної дисфункції та порушень мікроциркуляції в пацієнтів із критичною ішемією нижніх кінцівок та високим ризиком розвитку реперфузійно-реоксигенаційних ускладнень

Актуальність. Епідеміологічні дослідження свідчать, що критична ішемія нижніх кінцівок трапляється в 500–1000 пацієнтів на один мільйон населення на рік. В Україні щорічно проводиться близько 10 000 реконструктивних операцій із приводу оклюзійних уражень артерій нижніх кінцівок. Одночасно щорічно виконується близько 8–10 тис. ампутацій нижніх кінцівок на ґрунті атеросклерозу. Метою дослідження було вивчення можливості корекції ендотеліальної дисфункції та порушень мікроциркуляції в пацієнтів із хронічною критичною ішемією нижніх кінцівок та високим ризиком розвитку реперфузійно-реоксигенаційних ускладнень після реконструктивних операцій. Матеріали та методи. В основу роботи покладено аналіз комплексного обстеження та хірургічного лікування 220 хворих на облітеручий атеросклероз аорти та магістральних артерій нижніх кінцівок. Ендотеліальну дисфункцію оцінювали шляхом визначення рівня маркерів: Р-селектину, Е-селектину, тканинного активатора плазміногену, ендотеліну-1, молекули адгезії судинного ендотелію 1-го типу, циркулюючих ендотеліальних клітин. Результати. Порівнюючи рівень ендотеліальної дисфунції та стан мікроциркуляції в ранньому післяопераційному періоді в пацієнтів із спеціальною доопераційною підготовкою й без такої, можна говорити про потребу та ефективність перед­операційного застосування бета-блокатора небівололу, інгібітора АПФ периндоприлу аргініну та L-аргініну. Висновки. Застосування в передопераційному періоді бета-блокатора небівололу, інгібітора АПФ периндоприлу аргініну, L-аргініну та сольового гіперосмотичного гіпертонічного розчину декстрану в пацієнтів із високим ризиком реперфузійно-реоксигенаційних ускладнень дає можливість запобігти значним порушенням при розвитку ендотеліальної дисфункції та погіршенню функціонування мікроциркуляторного русла й забезпечити оксигенацію тканин на рівні 5,04 ± ,37 мм рт.ст. після реваскуляризації нижніх кінцівок.

Analyzing the driving forces of insulin stability in the basic amino acid solutions: A perspective from hydration dynamics.

Amino acids having basic side chains, as additives, are known to increase the stability of native-folded state of proteins, but their relative efficiency and the molecular mechanism are still controversial and obscure as well. In the present work, extensive atomistic molecular dynamics simulations were performed to investigate the hydration properties of aqueous solutions of concentrated arginine, histidine, and lysine and their comparative efficiency on regulating the conformational stability of the insulin monomer. We identified that in the aqueous solutions of the free amino acids, the nonuniform relaxation of amino acid-water hydrogen bonds was due to the entrapment of water molecules within the amino acid clusters formed in solutions. Insulin, when tested with these solutions, was found to show rigid conformations, relative to that in pure water. We observed that while the salt bridges formed by the lysine as an additive contributed more toward the direct interactions with insulin, the cation-π was more prominent for the insulin-arginine interactions. Importantly, it was observed that the preferentially more excluded arginine, compared to histidine and lysine from the insulin surface, enriches the hydration layer of the protein. Our study reveals that the loss of configurational entropy of insulin in arginine solution, as compared to that in pure water, is more as compared to the entropy loss in the other two amino acid solutions, which, moreover, was found to be due to the presence of motionally bound less entropic hydration water of insulin in arginine solution than in histidine or lysine solution.

An Evidence for a Novel Antiviral Mechanism: Modulating Effects of Arg-Glc Maillard Reaction Products on the Phase Transition of Multilamellar Vesicles.

Maillard reaction products (MRPs) of protein, amino acids, and reducing sugars from many foods and aqueous extracts of herbs are found to have various bioactivities, including antiviral effects. A hypothesis was proposed that their antiviral activity is due to the interaction with the cellular membrane. Aiming to estimate the possible actions of MRPs on phospholipid bilayers, the Arg-Glc MRPs were prepared by boiling the pre-mixed solution of arginine and glucose for 60 min at 100°C and then examined at a series of concentrations for their effects on the phase transition of MeDOPE multilamellar vesicles (MLVs), for the first time, by using differential scanning calorimetry (DSC) and temperature-resolved small-angle X-ray scattering (SAXS). Arg-Glc MRPs inhibited the lamellar gel–liquid crystal (Lβ-Lα), lamellar liquid crystal–cubic (Lα-QII), and lamellar liquid crystal–inverted hexagonal (Lα-HII) phase transitions at low concentration (molar ratio of lipid vs. MRPs was 100:1 or 100:2), but promoted all three transitions at medium concentration (100:5). At high concentration (10:1), the MRPs exhibited inhibitory effect again. The fusion peptide from simian immunodeficiency virus (SIV) induces membrane fusion by promoting the formation of a non-lamellar phase, e.g., cubic (QII) phase, and inhibiting the transition to HII. Arg-Glc MRPs, at low concentration, stabilized the lamellar structure of SIV peptide containing lipid bilayers, but facilitated the formation of non-lamellar phases at medium concentration (100:5). The concentration-dependent activity of MRPs upon lipid phase transition indiciates a potential role in modulating some membrane-related biological events, e.g., viral membrane fusion.

Next-Generation Sequencing for Determining the Effect of Arginine on Human Dental Biofilms Using an In Situ Model.

Oral biofilms are associated with caries, periodontal diseases, and systemic diseases. Generally, antimicrobial therapy is used as the first line of treatment for infectious diseases; however, bacteria in biofilms eventually develop antibiotic resistance. This study aimed to apply our in situ biofilm model to verify whether an arginine preparation is useful for plaque control. Ten healthy subjects who did not show signs of caries, gingivitis, or periodontitis were recruited. The dental biofilms from the subjects were obtained using our oral device before and after gargling with arginine solution for 4 weeks. We found that 8% arginine solution significantly increased the concentration of ammonium ions (NH4+) in vitro and in vivo in saliva (p < 0.05) and decreased the proportions of the genera Atopobium and Catonella in vivo. However, the viable count was unaffected by the mouthwash. Further, oral populations of the genera Streptococcus and Neisseria tended to increase with the use of arginine. Therefore, we concluded that using an 8% arginine solution decreased the NH4+ concentration in the oral cavity without affecting the number of viable bacteria, and that the diversity of oral bacterial flora changed. We suggest that arginine might help prevent mature biofilm formation.

Different Conditions for the Modification of Polycaprolactone Films with L-Arginine.

Poly-ε-caprolactone (PCL) is a biodegradable polymer used in regenerative medicine. Mesenchymal stem cells (MSCs) play an important role in the regeneration of different tissues. The hydrophobicity and neutrality of a PCL surface reduce MSCs’ adhesion and proliferation. In this study, PCL films were treated with arginine to improve surface hydrophilicity. The influences of arginine concentration, temperature, and solvent on PCL surface properties were investigated. PCL films treated with a solution of arginine in isopropyl alcohol were found to have the maximum number of amino groups. The greatest number of cells, 2 h after seeding, adhered to such films. It was shown that amino groups affect the interaction of cells with a modified surface and the hydrolysis reaction after treatment with isopropyl alcohol promotes the formation of adhesive focal contacts. Hence, our results illustrate that functional groups on the PCL surface after arginine solution treatment regulate MSC adhesion and focal contact formation.

Insights into the Sensitivity of Arginine Concentration to Preserve the Folded Form of Insulin Monomer under Thermal Stress.

Arginine, although popularly known as aggregation suppressor additive, has been found to quench proteins' structure and function by destabilizing their conformations. Driven by such controversial evidence, in this work we performed a series of atomistic molecular dynamics simulations of insulin monomer, a biologically active hormone protein, in arginine solution of varying concentrations (0.5, 1, and 2 M) at ambient and elevated temperature (400 K) to explore the arginine concentration driven structure-based stability of the protein. Our study reveals that the flexibility of the protein's structure is dependent on the arginine concentration, and among all the used solutions, 2 M arginine, a "neutral crowder" that mimics the cellular environment, can preserve the native folded form of the protein at ambient temperature in an excellent manner. Further, while the protein unfolds at 400 K in pure water, this solution worked satisfactorily to preserve the protein's folded conformation more firmly than the other solutions. The replica-exchange MD of insulin in 2 M arginine solution further supports the fact. In this aspect an important issue in molecular pharmacology is to identify and recognize the physical origin of the stability of a protein, i.e, in this case, how arginine directs the conformational flexibility of the protein and preserves its native folded form. We identified that the exclusion of arginine from the protein surface increases the local structuration of water around the protein, thereby preserving its "biological water" layer, and makes the protein more hydrated at 2 M concentration as compared to the other arginine solutions. Additionally, our microscopic investigation on the interactions of the protein-solvation layer revealed that the structural heterogeneity of the protein surface, arising from the differential physicochemical nature of the amino acid residues, controls the favorable formation of sluggish water-arginine mixed solvation layer at higher arginine concentration that helps the protein to maintain its structural rigidity. Importantly, apart from the protein-solvent hydrogen-bonding interactions, the anion-pi interactions, established between the carboxyl group of arginine and the aromatic amino acid residues of insulin, were recognized to facilitate the protein to maintain its native folded form at the experimental temperatures.

Arginine-mediated dissociation of single cells and cell sheets from a polystyrene culture dish.

Here, we report a novel non-enzymatic cell dissociation method, based on our finding that adherent cells dissociate rapidly from the polystyrene culture dish when incubated in an l- or d-arginine-containing solution. We also demonstrate the successful detachment of confluent NIH/3T3 cell monolayers from the culture dish as a cell sheet by the addition of an arginine solution.

Thermodynamics and solute-solvent interactions of lovastatin in an aqueous arginine solution

Lovastatin (LVS) is an effective therapeutic and prophylactic agent in several cardiovascular disorders. However, it has low bioavailability. This study investigated solute-solvent and solute-cosolute interactions and assessed thermodynamic parameters that contributed to LVS solubility enhancement in the presence of arginine (ARG) as a hydrotropic agent. The electrolytic conductance of LVS-ARG binary system was measured at temperatures from 298.15 K to 313.15 K. Conductometric parameters such as limiting molar conductance was evaluated. Additionally, thermodynamic parameters (ΔG0, ΔH0, ΔS0 and ES) involved in the association process of the solute in the aqueous solution of ARG solution were determined systematically. Solubility markedly improved 43-fold in the LVS-ARG complex compared to LVS alone. The analysed data from values of molar conductance and activation energy suggested favourable solubilisation, with a stronger solute-solvent interaction between LVS-ARG in water at higher temperatures. ARG and LVS complexation caused by strong molecular interactions was confirmed by spectral results. Hence, the addition of ARG as a co-solute was proven to enhance LVS solubility in water. The obtained data will ultimately enable the development of desired highly soluble, more efficient and safer LVS preparations.