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Tjandrawinata R.R.,Dexa Laboratories of Biomolecular science | Trisina J.,Dexa Laboratories of Biomolecular science | Rahayu P.,Dexa Laboratories of Biomolecular science | Prasetya L.A.,Dexa Laboratories of Biomolecular science | And 2 more authors.
Drug Design, Development and Therapy | Year: 2014

DLBS1033 is a bioactive protein fraction isolated from Lumbricus rubellus that tends to be unstable when exposed to the gastrointestinal environment. Accordingly, appropriate pharmaceutical development is needed to maximize absorption of the protein fraction in the gastrointestinal tract. In vitro, ex vivo, and in vivo stability assays were performed to study the stability of the bioactive protein fraction in gastric conditions. The bioactive protein fraction DLBS1033 was found to be unstable at low pH and in gastric fluid. The “enteric coating” formulation showed no leakage in gastric fluid–like medium and possessed a good release profile in simulated intestinal medium. DLBS1033 was absorbed through the small intestine in an intact protein form, confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) analysis. This result confirmed that an enteric coating formula using methacrylic acid copolymer could protect DLBS1033 from the acidic condition of the stomach by preventing the release of DLBS1033 in the stomach, while promoting its release when reaching the intestine. From the blood concentration–versus-time curve, 99mTc-DLBS1033 showed a circulation half-life of 70 minutes. This relatively long biological half-life supports its function as a thrombolytic protein. Thus, an enteric delivery system is considered the best approach for DLBS1033 as an oral thrombolytic agent. © 2014 Tjandrawinata et al.

Tjandrawinata R.R.,Dexa Laboratories of Biomolecular science | Trisina J.,Dexa Laboratories of Biomolecular science | Sunardi F.,Dexa Laboratories of Biomolecular science | Suhartono M.T.,Dexa Laboratories of Biomolecular science | Suhartono M.T.,Bogor Agricultural University
Journal of Biomedicine and Biotechnology | Year: 2011

The medicinal value of earthworm has been widely known since the history of Asian ancient medicine. This present study aims to determine the mechanism of action and effect of a standardized extract of Lumbricus rubellus named as DLBS1033. The fibrinogen degradation, antiplatelet aggregation, and ex vivo antithrombotic assay using human blood were performed to study antithrombotic activity. Fibrin plate and clot lysis assay were also done to examine thrombolytic properties. DLBS1033 was found to possess fibrinogenolytic activity on -, -, and -chain of fibrinogen. It also induced antiplatelet aggregation and prolonged blood clotting time, which further confirmed its antithrombotic properties. In addition, thrombolytic properties of DLBS1033 were shown with its fast and long-acting fibrinolytic activity, as well as its effective blood clot lysis activities. In conclusion, DLBS1033 conferred antithrombotic and thrombolytic action which could be used as a safe and promising oral thrombolytic drug. Copyright 2011 Jessica Trisina et al.

Gasong B.T.,Dexa Laboratories of Biomolecular science | Tjandrawinata R.R.,Dexa Laboratories of Biomolecular science
Asian Pacific Journal of Tropical Biomedicine | Year: 2016

Objective: To isolate new endophytic fungus from Phaleria macrocarpa (P. macrocarpa) that is able to produce E2.2 compound. Methods: Endophytic fungi were isolated from P. macrocarpa. Morphological and molecular identification was done to determine the species of the endophytic fungus. High performance liquid chromatography was used to determine the ability of this fungus to produce E2.2 compound and to quantify the total yield of E2.2 from fungal fermentation. Fermentation process was optimized by observing suitable medium, pH and length of fermentation process. Phloroglucinol and gallic acid addition were examined to determine the effect of each compound on E2.2 production. Results: One endophytic fungus was successfully isolated from P. macrocarpa plant. Morphological and molecular identification showed that it was a Colletotrichum gloeosporioides which belonged to Glomerellaceae family. This fungus showed highest production of E2.2 when incubated in potato dextrose broth with initial pH value of the medium at 5, and was incubated for 15 days. Phloroglucinol was found to better enhance E2.2 production. Conclusions: Colletotrichum gloeosporioides found in P. macrocarpa plant is promising as a potential alternative source of E2.2. © 2016 Hainan Medical University.

Anggadiredja K.,Bandung Institute of Technology | Tjandrawinata R.R.,Dexa Laboratories of Biomolecular science
Cardiovascular Toxicology | Year: 2015

DLBS1425 is a bioactive compound extracted from Phaleria macrocarpa, with anti-proliferative, anti-inflammatory and anti-angiogenic properties against cancer cells. The present study was aimed to assess cardiotoxicity of DLBS1425, compared to the mainstay regimen for breast cancer, 5-fluorouracil:doxorubicin:cyclophosphamide (FAC, given at 500/50/500 mg/m2). Treatment with FAC regimen at standard dose resulted in very severe toxicity, so mice had no chance to survive for more than 7 days following initial drug treatment. Furthermore, histological examination on the heart revealed severe muscular damage when mice were given the FAC regimen alone (severe toxicity). FAC as chemotherapeutic regimen exerted high toxicity profile to the cardiovascular cells in this experiment. Meanwhile, treatment with DLBS1425 alone up to a dose equivalent to as high as 300 mg three times daily in human had no hazardous consequences on the heart, hematological feature, as well as general safety. In the cardiovascular cells, DLBS1425 in the presence of FAC regimen (one-eight of the initial dose) gave protection to the cardiac muscle cells as well as other hematological features. Taken together, results of the present study suggest that DLBS1425 is safe when used as adjuvant therapy for breast cancer and may be even protective against cardiac cellular damage produced by chemotherapeutic regimen. © 2014, Springer Science+Business Media New York.

Tjandrawinata R.R.,Dexa Laboratories of Biomolecular science | Arifin P.F.,Dexa Laboratories of Biomolecular science | Tandrasasmita O.M.,Dexa Laboratories of Biomolecular science | Rahmi D.,Dexa Laboratories of Biomolecular science | Aripin A.,Dexa Laboratories of Biomolecular science
Journal of Experimental Therapeutics and Oncology | Year: 2010

Phaleria macrocarpa (Scheff.) Boerl. (Thymelaeaceae), an Indonesian native plant, has been used to treat various diseases in Indonesia. DLBS1425, a standardized extract of flesh fruit of Phaleria macrocarpa, is hypothesized to have anti-cancer activities. Anti-proliferative and induction of apoptosis conferred by DLBS1425 on breast cancer cells, MDA-MB-231 and MCF-7 cells were investigated. DLBS1425 showed an inhibition of proliferation in both cell lines. Induction of apoptosis was shown by DNA fragmentation, activation of caspase 9, and regulation of Bax and Bcl-2 at the mRNA level. DLBS1425 downregulated COX-2, cPLA2, and VEGF-C mRNA expressions. DLBS1425 also down-regulated c-fos and HER-2/neu mRNA expression in TPA- or fatty acid-induced MDA-MB-231 cells. These findings demonstrate that DLBS1425 has anti-proliferative, anti-inflammatory, and anti-angiogenic properties, which make it pharmacologically ideal for the prevention and/or treatment of breast cancer. © 2010 Old City Publishing, Inc.

Berlian G.,Dexa Laboratories of Biomolecular science | Tandrasasmita O.M.,Dexa Laboratories of Biomolecular science | Tjandrawinata R.R.,Dexa Laboratories of Biomolecular science
Asian Pacific Journal of Tropical Biomedicine | Year: 2016

Objective To verify that Proliverenol has a potential ability in protecting cells from ethanol-induced hepatotoxicity. Methods Activity of Proliverenol against ethanol-induced apoptosis was evaluated at mRNA and protein levels in HepG2 cell exposed to Proliverenol for 1 and 3 h. Results Proliverenol conferred hepatoprotective activity through increasing cell survival up to 53%–69% via up-regulation of APEX1 DNA repair enzyme for 3.0–4.7 fold and down-regulating of nuclear factor-κB, tumor necrosis factorα and caspase-8 expression, allowing them to prevent 4.5–6.9 fold of alanine aminotransferase (ALT) leakage in HepG2 cells. Our finding revealed that Proliverenol repressed expression of ALT, which is significantly important as possible alternative mechanism for increased blood transaminase activities. In addition, the result also showed that caspase-8 pathway seemed to be involved in the molecular pathway rather than directly inducing mitochondrial damage. Conclusions The data support our hypothesis that Proliverenol has a potential ability in protecting cells from ethanol-induced hepatotoxicity. We propose that Proliverenol provides hepatoprotective activity through up-regulating expression of APEX1 that repress DNA fragmentation, and down-regulating expression of nuclear factor-κB, tumor necrosis factorα and caspase-8, which therefore repress ALT leakage and its expression. © 2016 Hainan Medical University

PubMed | Dexa Laboratories of Biomolecular science and Bandung Institute of Technology
Type: Journal Article | Journal: Scientia pharmaceutica | Year: 2016

A lectin-like protein of unknown function designated as LSMT was recently discovered in the edible mushroom Agaricus bisporus. The protein shares high structural similarity to HA-33 from Clostridium botulinum (HA33) and Ricin-B-like lectin from the mushroom Clitocybe nebularis (CNL), which have been developed as drug carrier and anti-cancer, respectively. These homologous proteins display the ability to penetrate the intestinal epithelial cell monolayer, and are beneficial for oral administration. As the characteristics of LSMT are unknown, a structural study in silico was performed to assess its potential pharmaceutical application. The study suggested potential binding to target ligands such as HA-33 and CNL although the nature, specificity, capacity, mode, and strength may differ. Further molecular docking experiments suggest that interactions between the LSMT and tested ligands may take place. This finding indicates the possible use of the LSMT protein, initiating new research on its use for pharmaceutical purposes.

PubMed | Dexa Laboratories of Biomolecular science and Bandung Institute of Technology
Type: | Journal: International journal of biological macromolecules | Year: 2017

Recombinant hybrid Manganese superoxide dismutase from Staphyloccus saphropyticus/S. equorum (rMnSODSeq) exhibits stability at high temperatures. The enzyme occurs as a dimer that dissociates around 52C prior to unfolding of the monomer around 64C, demonstrating contribution of the dimeric form to stability. Here, structure - activity relationship of rMnSODSeq was evaluated on the basis of its activity and stability in the presence of inhibitors, NaCl, denaturants, detergents, reducing agents, and at different pH values. The activity was evaluated at both 37C and 52C, which the latter is the temperature for dissociation of the dimer. Dimer to monomer transition coincided with significant decrease in residual activity at 52C. However, the activity assay results at 52C and 37C suggest spontaneous re-association of the monomer into dimer. Intriguingly, various new species with melting temperature (T

PubMed | Dexa Laboratories of Biomolecular science and Bandung Institute of Technology
Type: Journal Article | Journal: International journal of pharmaceutics | Year: 2016

We report novel pharmaceutical cocrystal of a popular antipyretic drug paracetamol (PCA) with coformer 5-nitroisophhthalic acid (5NIP) to improve its tabletability. The cocrystal (PCA-5NIP at molar ratio of 1:1) was synthesized by solvent evaporation technique using methanol as solvent. The physicochemical properties of cocrystal were characterized by powder X-ray diffraction (PXRD), differential scanning calorimetry (DSC), thermogravimetry analysis (TGA), fourier transform infrared spectroscopy (FTIR), hot stage polarized microscopy (HSPM) and scanning electron microscopy (SEM). Stability of the cocrystal was assessed by storing them at 40C/75% RH for one month. Compared to PCA, the cocrystal displayed superior tableting performance. PCA-5NIP cocrystal showed a similar dissolution profile as compared to PCA and exhibited good stability. This study showed the utility of PCA-5NIP cocrystal for improving mechanical properties of PCA.

PubMed | Dexa Laboratories of Biomolecular science, Bandung Institute of Technology and University of Gottingen
Type: Journal Article | Journal: The protein journal | Year: 2016

A recombinant hybrid of manganese dependent-superoxide dismutase of Staphylococcus equorum and S. saprophyticus has successfully been overexpressed in Escherichia coli BL21(DE3), purified, and characterized. The recombinant enzyme suffered from degradation and aggregation upon storage at -20 C, but not at room temperature nor in cold. Chromatographic analysis in a size exclusion column suggested the occurrence of dimeric form, which has been reported to contribute in maintaining the stability of the enzyme. Effect of monovalent (Na(+), K(+)), divalent (Ca(2+), Mg(2+)), multivalent (Mn(2+/4+), Zn(2+/4+)) cations and anions (Cl(-), SO4 (2-)) to the enzyme stability or dimeric state depended on type of cation or anion, its concentration, and pH. However, tremendous effect was observed with 50 mM ZnSO4, in which thermostability of both the dimer and monomer was increased. Similar situation was not observed with MnSO4, and its presence was detrimental at 200 mM. Finally, chelating agent appeared to destabilize the dimer around neutral pH and dissociate it at basic pH. The monomer remained stable upon addition of ethylene diamine tetraacetic acid. Here we reported unique characteristics and stability of manganese dependent-superoxide dismutase from S. equorum/saprophyticus.

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