{"title":"Clinical Pharmaceutical Care, Medical Laboratory Imaging, NuclearMedicine: A Synergy to Improve Clinical Outcomes and Reducing Costs","authors":"M. Luisetto","doi":"10.21065/1920-4159.1000E112","DOIUrl":"https://doi.org/10.21065/1920-4159.1000E112","url":null,"abstract":"The purpose of this paper is to analyse the advantages and roles played by clinical ward pharmacists as members of a medical team with physicians. Using the data obtained by medicine laboratory and imaging, as instruments to monitor the therapy to improve patients clinical outcomes, and to a better costs containment quality of life and safety.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"17 4 1","pages":"1-2"},"PeriodicalIF":0.0,"publicationDate":"2016-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74974310","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Coexpression of Genetically Engineered Cyt b5-CYP3A4 Fusion Protein withPOR in Sf9 Insect Cells and Functional Characterization of the ExpressedProducts in vitro","authors":"Zhangming Xie, Shabbir Ahmed, Wenhui Liu, Si-si Kong, Yingchun Xu, Ting Liu, Shuqing Chen","doi":"10.21065/1920-4159.1000223","DOIUrl":"https://doi.org/10.21065/1920-4159.1000223","url":null,"abstract":"Human cytochrome P450 3A4 (CYP3A4) is the most abundant phase I drug-metabolizing enzyme in the liver, and approximately 50% of drugs on the market are metabolized by CYP3A4. Therefore, many in vitro studies relied on recombinant CYP3A4 as screening tool to evaluate potential drug-drug interactions (DDIs) in vivo. However, limited information regarding recombinant CYP3A4 with high catalytic activity is available. So, the present study aimed to obtain recombinant CYP3A4 with high catalytic activity and to characterize its functions in vitro. To enhance the catalytic activities of heterologously expressed CYP3A4, the enzyme was fused to cytochrome b5 (b5) tail-to-head, and the fused enzyme was inserted together with NADPH–P450 reductase (POR) into a single plasmid to achieve a simultaneous expression in sf9 cells. Here, substrate binding affinities, enzymatic activities and applications in in vitro DDIs of the fused enzyme were investigated. The dissociation constant Kd of POR-cyt b5CYP3A4 was 8.3 ± 0.87 μmol/L, the Clint (Clint=Vmax/Km) was 8.57 mL/min/g protein for POR-cyt b5CYP3A4 in the metabolism of testosterone and 150.3 mL/min/g protein for midazolam. In addition, the inhibitory constant Ki of ketoconazole on testosterone metabolism was 0.013 ± 0.0038 μmol/L. The present results suggested significantly increased substrate binding affinity and enzymatic activity for the fused enzyme. Thus, the construct could be helpful for studying drug metabolisms and DDIs investigation associated with CYP3A4 in vitro. In addition, simultaneous expression of the fused enzyme and POR could provide more reproducible results based on a more stable molar ratio of CYP3A4/POR/b5.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"98 2 1","pages":"1-6"},"PeriodicalIF":0.0,"publicationDate":"2016-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79461682","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A Short Review on Chiral Alcohols Verses Bio-Catalysis","authors":"S. Chittamuru, B. Reddy, A. Rao","doi":"10.21065/1920-4159.1000222","DOIUrl":"https://doi.org/10.21065/1920-4159.1000222","url":null,"abstract":"Catalyst is a chemical molecule or metal substance which enhances the rate of reaction is called catalyst, the catalyst present in the living organisms to carryout biochemical reactions or metabolic pathways. Exames oxidoreductases, lyases, ligages, proteases, hydrolases, esterases, pectinases etc. are Different methodologies available in synthesis of chiral molecules chemical/biocatalysis. The enormous potential of biocatalysts (microorganisms and enzymes) in synthesis of chiral molecules in mild conditions (pH and temperate) with high chemo-, regio-, enantio and functional selectivity with decrease formation of by-products, with short reaction steps (reactions which are not easily conducted classical organic reactions) (Long chemical processes with tedious blocking and de-blocking steps). Thus the use of biocatalyst has attracted a great attention from the green chemistry perspective (expensive chiral reagents/ environmentally hazardous heavy metals). Biocatalysts are well known for their enzymatic activity towards numerous reactions ranging from in-vivo living cells (biochemical pathways) to in-vitro chemical reactions (reduction and transesterification) with enantiomeric purity and specificity. In this review the discussion is about synthesis of chiral using different kinds of biocatalysts. Daucus Carota, Pisum Sativa, Novazyme P-435, as biocatalysts for chiral alcohols.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"79 1","pages":"1-4"},"PeriodicalIF":0.0,"publicationDate":"2016-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75359266","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
E. Ruiz, Covadonga Álvarez, J. Rodriguez, S. Durán, S. Durán, Dellias Pm
{"title":"New Multi-Particle Systems for Colon-Targeted Meloxicam","authors":"E. Ruiz, Covadonga Álvarez, J. Rodriguez, S. Durán, S. Durán, Dellias Pm","doi":"10.21065/1920-4159.1000221","DOIUrl":"https://doi.org/10.21065/1920-4159.1000221","url":null,"abstract":"Meloxicam (MLX) is a non-steroidal anti-inflammatory drug (NSAIDs) from the Oxicam family. This group of NSAIDs has been highly used in the treatment of rheumatoid arthritis and post-operative inflammation and is known as good antioxidants. Recently, their activity in chemoprevention, chemo-suppression, UV-sensitization and UVprotection was also identified. MLX has been described as a COX-2 selective inhibitor. Its use has some advantages regarding to its selectivity, namely, less adverse effects as gastrointestinal aggression and anticlotting activity. As MLX is better absorbed in colon and its properties against colon cancer and colonic inflammatory diseases are being studied, it is interesting to investigate a new MLX formulation for colonic delivery. We are studying the solubility and the dissolution of different combined formulations at pH 1.2, 6.8 and 7.4 to mimic their absorbance in the colon. These formulations are composed by different excipients that provide pH and time-dependent deliveries such as cellulose (Metolose®) and methacrylic acid esters with quaternary ammonium groups (EUDRAGIT® RS 30D, EUDRAGIT® FS 30D and EUDRAGIT® NM 30D).","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"43 1 1","pages":"1-3"},"PeriodicalIF":0.0,"publicationDate":"2016-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79965435","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
S. A. Mohamoud, Teshager Aklilu Yesuf, Eskinder Ayalew Sisay
{"title":"Utilization Assessment of Surgical Antibiotic Prophylaxis at Ayder Referral Hospital, Northern Ethiopia","authors":"S. A. Mohamoud, Teshager Aklilu Yesuf, Eskinder Ayalew Sisay","doi":"10.4172/1920-4159.1000220","DOIUrl":"https://doi.org/10.4172/1920-4159.1000220","url":null,"abstract":"Introduction: Surgical site infection represents a significant burden in terms of patients’ morbidity, mortality and hospital costs which can be prevented using prophylaxis. \u0000 \u0000Objective: To assess rate of compliance to Surgical Antibiotic Prophylaxis (SAP) guidelines at Ayder Referral Hospital (ARH). \u0000 \u0000Method: Prospective cross-sectional study was conducted from 12th March to 28thApril, 2015. Data were collected using data abstraction checklist for all patients who underwent surgery and met inclusion criteria. SAP Guidelines and CDC Wound Classification were used as data assessment protocols. Epidata 3.1 and SPSS 16 were used for data entry and analysis of descriptive statistics. \u0000 \u0000Results: A total of 196 patients with mean age of 37.84 years were recruited (female, 58.7%). Of these, 62.2% received SAP but prophylaxis was needed in 58.2%. The total compliance to SAP guideline was 21.9% and 25% for national Standard Treatment Guideline (STG) and American Society of Health-system Pharmacist (ASHP) guideline respectively. Selection of SAP (national STG 100% versus ASHP Guideline 89.5%) was the most deviated parameter from SAP guidelines followed by duration (63.5%), indication (19.4%) and dose (10.4%). Most commonly used agent was ceftriaxone (85.2%). \u0000 \u0000Conclusion: Current practice of ARH is hugely divergent from SAP guidelines. Use of broader spectrum antibiotics for an extended period was common.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"42 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2016-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87011297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Synthesis Characterization and Biological Influence of Some NewlySynthesized Mix ligand Chelates","authors":"ya Dr","doi":"10.4172/1920-4159.1000219","DOIUrl":"https://doi.org/10.4172/1920-4159.1000219","url":null,"abstract":"Objective: A series of mixed ligand chelates of d10 were synthesized expending 3TC a potent nucleoside analogue and ACV, is a guanosine analogue antiviral drug. \u0000Methods: The synthesized chelates were characterized by IR, Mass spectra, TGA analysis and Elemental analysis and were evaluated for their anti-fungal activity against a panel of two pathogenic fungal strains namely, Aspergillus niger, and Candida albicans by Broth-dilution method, antibacterial activity against E. coli, P. aeruginosa, S. aureus, S. pyogenus. \u0000Results: All the compounds showed significant inhibitory activity against the microorganism. Anti-bacterial activity was determined using Ampicillin as a standard and antifungal activity was determined using standard Greseofulvin. \u0000Conclusion: Out of all the chelates, the chelate of Cd2+ exhibited promising antimicrobial activity as a whole.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"4 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2016-04-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90016732","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
C. Selvakkumar, K. Muthusamy, Sathishkumar Chinnasamy
{"title":"Nanopeptides: Non-Covalent Interactions in Chemistry and Biological Functions","authors":"C. Selvakkumar, K. Muthusamy, Sathishkumar Chinnasamy","doi":"10.4172/1920-4159.1000218","DOIUrl":"https://doi.org/10.4172/1920-4159.1000218","url":null,"abstract":"The interactions involving the side chains of weakly polar aromatic amino acid residues, e.g., Phenylalanine (Phe), Tyrosine (Tyr) and Tryptophan (Trp) generally reside at the interior of proteins and help in the stabilization of globular protein structures. The aromatic electron cloud of the aromatic rings of these amino acids are delocalized on both sides of the planer rings, so that there is a small partial negative charge on the face and a small partial positive charge on the hydrogen atoms of the edge, which leads to the possibility of electrostatic interactions. These interaction play a vital role nanofiber based vaccine adjuvants, and cocaine vaccine development and increasing interest and structure based drug development. Apart from electrostatic forces, aromatic interactions also consist of van der Waals and hydrophobic forces. These weakly polar interactions are enthalpically comparable to a hydrogen bond. Protein engineering methods have revealed that introducing aromatic pairs and aromatic clusters increases the thermal stability of proteins and it has been demonstrated that the introduction of an additional aromatic interaction improved the thermophilicity and thermostability of the family of 11 xylanase. These weakly polar interactions also have a significant role in the stability of DNA. Different types of weakly polar interactions involving the aromatic side chains are discussed below.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"33 1","pages":"1-8"},"PeriodicalIF":0.0,"publicationDate":"2016-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91380530","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Design, Synthesis and Development of Stereo Chemical Constraints into β -Amino Acid Residues: Gabapentin Structural Data Role in Nerve Pain Medication","authors":"Saravana Kumar Kailasam Mani, R. Narayanasamy","doi":"10.4172/1920-4159.1000217","DOIUrl":"https://doi.org/10.4172/1920-4159.1000217","url":null,"abstract":"Over the last 15 years, a growing body of work in the literature has focused on the folded structures formed by peptide sequences containing backbone homologated residues. The work of Seebach in Zurich, and Gellman in Madison, established that oligomers of β amino acid residues can form novel helical structures in solution and in the solid state. These peptides are highly useful for nnaovaccine development. Two distinct types of hydrogen bonded helical structures were demonstrated in these studies for oligomeric β peptides. The C12 helix which is an analog of the canonical 310 helical structure in “all α” sequences, has the same hydrogen bond directionality (C = Oi …..H-Ni+3). The second helical form, the C14 helix, has the opposite directionality (C = Oi …..H-Ni+4), which is unprecedented in α peptide sequences.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"12 1","pages":"1-3"},"PeriodicalIF":0.0,"publicationDate":"2016-04-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79548243","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Conformational Angles and Properties of andOmega;-Amino Acids in ProteinFolding","authors":"VS Saravana Mani, R. Narayanasamy","doi":"10.4172/1920-4159.1000216","DOIUrl":"https://doi.org/10.4172/1920-4159.1000216","url":null,"abstract":"The conformational properties of β-amino acid residues are based on three degrees of freedom: φ (N Cβ), θ (Cβ Cα), ψ (Cα CO). Similarly, the conformational variabilities of γand δamino acid residues are defined as four [φ (N Cγ), θ1 (Cγ Cβ), θ2 (Cβ Cα), ψ (Cα CO)] and five [[φ (N Cδ), θ1 (Cδ Cγ), θ2 (Cγ Cβ), θ3 (Cβ Cα), ψ (Cα CO)] degrees of freedom, respectively [8]. Figure 1a illustrates the comparison of backbone torsion angles in α-, β-, γand δ-amino acid residues.","PeriodicalId":15238,"journal":{"name":"Journal of Applied Pharmacy","volume":"1 1","pages":"1-2"},"PeriodicalIF":0.0,"publicationDate":"2016-04-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89021866","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}