Graft polymerization of glycidylmethacrylate onto coralline hydroxyapatite.

Graft polymerization of glycidylmethacrylate (GMA) onto coralline hydroxyapatite (CHA) was carried out using potassium persulfate (K2S2O8) and sodium metabisulfite (Na2S2O5) as initiators in aqueous medium. To optimize the reaction conditions for getting maximum grafting yield, the concentrations of backbone, monomer, initiator, temperature and time were varied. The percent grafting was found to increase initially and then gradually decrease with respect to reaction parameters. The results obtained imply that the optimum temperature and time was 60 degrees C and 180 min, respectively, to obtain higher grafting yield. The grafting results have been discussed and a mechanism involved in the grafting of GMA onto CHA is described. The grafted materials were analyzed with Fourier transform infrared (FT-IR) spectroscopy and X-ray diffraction (XRD) measurements. The results of FT-IR confirmed the presence of epoxy group on the grafted CHA. The XRD pattern showed that there was no secondary phase in the apatite lattice due to chemical modification.

Preparation, characterization and in vitro release of gentamicin from coralline hydroxyapatite-gelatin composite microspheres.

Composite microspheres have been prepared from bioactive ceramics such as coralline hydroxyapatite [CHA, Ca10(PO4)6(OH)2] granules, a biodegradable polymer, gelatin and an antibiotic, gentamicin. In our earlier work, we have shown a gentamicin release from CHA granules--chitosan composite microspheres. In the present investigation, an attempt was made to prepare the composite microspheres containing coralline hydroxyapatite and gelatin (CHA-G), which were prepared by the dispersion polymerization technique and the gentamicin was incorporated by the absorption method. The crystal structure of the composite microspheres was analyzed using X-ray powder diffractometer. The Fourier transformed infrared spectrum clearly indicated the presence of amide and hydroxyl groups in the composite microspheres. Scanning electron micrographs and optical micrographs show that the composite microspheres are spherical in shape and porous in nature. The particle size of composite microspheres was analyzed and the average size was found to be 16 microm. The thermal behavior of composite microspheres was studied using thermogravimetric analysis and differential scanning calorimetric analysis. The cumulative in vitro release profile of gentamicin from composite microspheres showed near zero order patterns.

Synthesis and characterization of functional gradient materials using Indian corals.

The partial conversion of coralline hydroxyapatite (HA) into tricalcium phosphate (TCP) catalyzed by the thermal decomposition of silver oxide was investigated. The thermal analysis of HA powder mixed with 5 mol % Ag2O indicated the decomposition of silver oxide to be around 550 degrees C in the presence of HA. Subsequently a functional gradient structure was formed by spreading silver oxide on one surface of the HA compact of diameter 10 mm and then firing at 700 degrees C in air. The X-ray powder diffraction analysis confirmed the formation of alpha-TCP induced by the Ag2O decomposition. The content of alpha-TCP of the sintered pellet was found to decrease with the increasing depth from the surface of the pellet. In vitro solubility study in phosphate buffer of pH 7.2 showed the stability of the biphasic material as in between HA and TCP.

Preparation and characterization of pH-sensitive proteinoid microspheres for the oral delivery of methotrexate.

Prot A7, a polypeptidic proteinoid composed of seven different amino acids, was synthesized and microspheres of 1-5 microm size were prepared by the self-assembly process. The morphological characterization of the microspheres was carried out using optical microscopy and SEM (scanning electron microscopy). Emphasis also has been made on studying the mechanism behind the microsphere formation and to relate it with the conformation of the polypeptide. These self-assembled microspheres were found to be pH-sensitive in aqueous medium. The suitability of the Prot A7 microspheres as a carrier for gastric irritant drugs was verified by choosing methotrexate (MTX) as a model drug. MTX was entrapped in proteinoid microspheres and its utility for the oral delivery system was verified by carrying out the drug dissolution studies in simulated gastric medium (pH 1.2) and neutral medium of the blood (pH 7) under physiological conditions. The pH responsive dissolution behaviour of the microspheres was clarified.

Some characteristics of collagen-heparin complex.

In various forms of purified collagen (powder of insoluble collagen from bovine skin, fibers from rat tail tendons, membrane from bovine gut), carboxyl groups were activated by carbodiimide to allow covalent binding of heparin. Collagen powder and collagen fibers from rat tail tendons were also incubated in a heparin solution under the same reaction conditions but without carbodiimide present to account for other forms of collagen-heparin interaction. It was found that the linkage of heparin to collagen formed in the presence of carbodiimide is stable, as heparin was minimally extractable by 0.2M buffers with a pH ranging from 5 to 9. Collagen powder incubated with heparin in the absence of carbodiimide released heparin almost completely into Tris buffer of pH 9.0. As a consequence of covalent binding of heparin to collagen, the collagen fibers became more stable as shown by their significantly reduced swelling capacity and significantly increased shrinkage temperature. Collagen fibers interacted with heparin in the absence of carbodiimide also showed some stabilization of their structure, which was, however, significantly less than with carbodiimide reaction. By two independent methods it was shown that heparin linked to collagen by a stable bond retains its anticoagulant activity. It is concluded that, in the presence of carbodiimide, heparin covalently binds to collagen thus forming an antithrombogenic surface. At the same time, collagen is crosslinked. Incubation of collagen in the solution of heparin without carbodiimide also stabilizes collagen structure, but to a significantly lesser degree. Such a linkage is unstable as heparin dissociates and is readily extractable into 0.2M Tris buffers with pH 7-9.