Progress in Pharmacokinetics and Pharmacodynamics - I
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Linezolid - Tigecycline
Linezolid - Tigecycline Paul M. Tulkens, MD, PhD Cellular and Molecular Pharmacology Louvain Drug Research Institute Catholic University of Louvain, Brussels, Belgium With the support of Wallonie-Bruxelles-International 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 1 Dong-A pharmaceuticals and tedizolid: step #1 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 2 Mode of action: • Protein synthesis inhibition: LZD binds to the 23S portion of the ribosomal 50S subunit (the centre of peptidyl transferase activity) → no initial complex 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 3 RNA interaction Karen L. Leach et al, Molecular Cell (2007) 26,393-402 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 4 Spectrum of activity No useful activity against other Gram-negative organisms because of constitutive efflux ! 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 5 Registered clinical indications Linezolid is often used off-label (endocarditis, osteomyelitis, ….) in pace of vancomycin 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 6 Linzezolid: mechanism of resistance 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 7 Can linzolid induce resistance ? 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 8 Linzolid can induce resistance… Locke et al. Antimicrob Agent Chemother 2009;53:5265-5274. 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 9 Linezolid pharmacokinetics 12-11-2015 WBI - HUP Cooperation - Bach Mai Hospital 10 Linezolid human pharmacokinetics Oral therapeutic doses (600mg linezolid q12h for 21 days) Linezolid Tedizolid MIC 90 MIC90 Muñoz et al. ECCMID 2010; P1594 Flanagan SD, et al. Pharmacotherapy 2014;34(3):240–250. -
Consideration of Antibacterial Medicines As Part Of
Consideration of antibacterial medicines as part of the revisions to 2019 WHO Model List of Essential Medicines for adults (EML) and Model List of Essential Medicines for children (EMLc) Section 6.2 Antibacterials including Access, Watch and Reserve Lists of antibiotics This summary has been prepared by the Health Technologies and Pharmaceuticals (HTP) programme at the WHO Regional Office for Europe. It is intended to communicate changes to the 2019 WHO Model List of Essential Medicines for adults (EML) and Model List of Essential Medicines for children (EMLc) to national counterparts involved in the evidence-based selection of medicines for inclusion in national essential medicines lists (NEMLs), lists of medicines for inclusion in reimbursement programs, and medicine formularies for use in primary, secondary and tertiary care. This document does not replace the full report of the WHO Expert Committee on Selection and Use of Essential Medicines (see The selection and use of essential medicines: report of the WHO Expert Committee on Selection and Use of Essential Medicines, 2019 (including the 21st WHO Model List of Essential Medicines and the 7th WHO Model List of Essential Medicines for Children). Geneva: World Health Organization; 2019 (WHO Technical Report Series, No. 1021). Licence: CC BY-NC-SA 3.0 IGO: https://apps.who.int/iris/bitstream/handle/10665/330668/9789241210300-eng.pdf?ua=1) and Corrigenda (March 2020) – TRS1021 (https://www.who.int/medicines/publications/essentialmedicines/TRS1021_corrigenda_March2020. pdf?ua=1). Executive summary of the report: https://apps.who.int/iris/bitstream/handle/10665/325773/WHO- MVP-EMP-IAU-2019.05-eng.pdf?ua=1. -
WO 2010/025328 Al
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date 4 March 2010 (04.03.2010) WO 2010/025328 Al (51) International Patent Classification: (81) Designated States (unless otherwise indicated, for every A61K 31/00 (2006.01) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, (21) International Application Number: CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, DO, PCT/US2009/055306 DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, (22) International Filing Date: HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, 28 August 2009 (28.08.2009) KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, (25) Filing Language: English NO, NZ, OM, PE, PG, PH, PL, PT, RO, RS, RU, SC, SD, (26) Publication Language: English SE, SG, SK, SL, SM, ST, SV, SY, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, ZW. (30) Priority Data: 61/092,497 28 August 2008 (28.08.2008) US (84) Designated States (unless otherwise indicated, for every kind of regional protection available): ARIPO (BW, GH, (71) Applicant (for all designated States except US): FOR¬ GM, KE, LS, MW, MZ, NA, SD, SL, SZ, TZ, UG, ZM, EST LABORATORIES HOLDINGS LIMITED [IE/ ZW), Eurasian (AM, AZ, BY, KG, KZ, MD, RU, TJ, —]; 18 Parliament Street, Milner House, Hamilton, TM), European (AT, BE, BG, CH, CY, CZ, DE, DK, EE, Bermuda HM12 (BM). -
Computational Antibiotics Book
Andrew V DeLong, Jared C Harris, Brittany S Larcart, Chandler B Massey, Chelsie D Northcutt, Somuayiro N Nwokike, Oscar A Otieno, Harsh M Patel, Mehulkumar P Patel, Pratik Pravin Patel, Eugene I Rowell, Brandon M Rush, Marc-Edwin G Saint-Louis, Amy M Vardeman, Felicia N Woods, Giso Abadi, Thomas J. Manning Computational Antibiotics Valdosta State University is located in South Georgia. Computational Antibiotics Index • Computational Details and Website Access (p. 8) • Acknowledgements (p. 9) • Dedications (p. 11) • Antibiotic Historical Introduction (p. 13) Introduction to Antibiotic groups • Penicillin’s (p. 21) • Carbapenems (p. 22) • Oxazolidines (p. 23) • Rifamycin (p. 24) • Lincosamides (p. 25) • Quinolones (p. 26) • Polypeptides antibiotics (p. 27) • Glycopeptide Antibiotics (p. 28) • Sulfonamides (p. 29) • Lipoglycopeptides (p. 30) • First Generation Cephalosporins (p. 31) • Cephalosporin Third Generation (p. 32) • Fourth-Generation Cephalosporins (p. 33) • Fifth Generation Cephalosporin’s (p. 34) • Tetracycline antibiotics (p. 35) Computational Antibiotics Antibiotics Covered (in alphabetical order) Amikacin (p. 36) Cefempidone (p. 98) Ceftizoxime (p. 159) Amoxicillin (p. 38) Cefepime (p. 100) Ceftobiprole (p. 161) Ampicillin (p. 40) Cefetamet (p. 102) Ceftoxide (p. 163) Arsphenamine (p. 42) Cefetrizole (p. 104) Ceftriaxone (p. 165) Azithromycin (p.44) Cefivitril (p. 106) Cefuracetime (p. 167) Aziocillin (p. 46) Cefixime (p. 108) Cefuroxime (p. 169) Aztreonam (p.48) Cefmatilen ( p. 110) Cefuzonam (p. 171) Bacampicillin (p. 50) Cefmetazole (p. 112) Cefalexin (p. 173) Bacitracin (p. 52) Cefodizime (p. 114) Chloramphenicol (p.175) Balofloxacin (p. 54) Cefonicid (p. 116) Cilastatin (p. 177) Carbenicillin (p. 56) Cefoperazone (p. 118) Ciprofloxacin (p. 179) Cefacetrile (p. 58) Cefoselis (p. 120) Clarithromycin (p. 181) Cefaclor (p. -
Tigecycline: a Igecycline
Molecules of the Millennium Tigecycline: A novel glycylcycline antibioticantibiotic Tetracycline antibiotics were first isolated at Lederle to occur.[5] Tigecycline is also active against organisms that Laboratories in 1945 and represented a significant display efflux-based resistance, which may be because of the advancement in the treatment of many infections. However, inability of the glycylcyclines to induce tetracycline efflux due to an increased incidence of resistance among various proteins, or because the efflux protein cannot export bacteria, the use of tetracyclines has been relegated to second tigecycline.[6] and third-line categories for most clinical indications. The two The binding site of tigecycline on the ribosome is common major mechanisms of resistance include tetracycline efflux to tetracyclines, but tigecycline binds 5-fold more strongly to and ribosomal protection, where tetracycline is prevented from the ribosome than tetracyclines and this enhanced binding is, binding to the ribosome. Research to find tetracycline probably, responsible for overcoming the ribosomal protection analogues, that circumvented these resistance mechanisms, mechanisms of tetracycline resistance.[5] The action of has led to the development of a novel group of drugs called tigecycline is bacteriostatic in nature, which is likely due to its glycylcyclines, the most promising compound being the 9-tert reversible interaction with the ribosome.[5] Its efficacy suggests butyl glycyclamido derivative of minocycline-tigecycline (GAR that traditional thinking about using bacteriostatic drugs in 936). treating serious infections needs to be revised.[7] Chemistry Antimicrobial activity The nucleus consists of four linear fused tetracyclic rings In vitro antibacterial activity of tigecycline has been and there is the addition of N, N-dimethylglycylamido (DMG) assessed against clinical isolates as a part of ongoing TEST group at C-9 position of minocycline.[1] initiative (Tigecycline Evaluation Surveillance Trial). -
Antibiotic Resistance Pattern to Different Isolates in Al-Hillah City, Iraq
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by International Institute for Science, Technology and Education (IISTE): E-Journals Journal of Natural Sciences Research www.iiste.org ISSN 2224-3186 (Paper) ISSN 2225-0921 (Online) Vo l.3, No.3, 2013 Pseudomonas aeruginosa: Antibiotic resistance pattern to different isolates in Al-Hillah city, Iraq Ali Hussein Al-Marzoqi1* (Corresponding author), and Zahraa Mohammad Al Taee2 1. College of Science for women, Babylon University, PO box 435, Al-Hillah city, Babylon, Iraq. Tel: 009647710336121 E-mail: [email protected] 2. College of Science, Babylon University * E-mail of the corresponding author: [email protected] Abstract Aim: Pseudomonas aeruginosa (Ps. aeruginosa) considered as most important bacteria which can isolated from various kinds of infection. This study tries to survey the infections caused by Ps. aeruginosa especially medical and surgical care units and try to reveal the antimicrobial agents susceptibility against Ps. aeruginosa. Material and Method: This study was conducted during September 2012 to February 2013. During this period total of 285 samples were tested and showed growth of bacteria. The isolates of Pseudomonas aeruginosa were selected on the basis of their growth on Nutrient agar pigmented and non-pigmented colonies with oxidase positive and on routine MacConkey medium which showed lactose Non-fermenting pale colonies. Antimicrobial susceptibility of all the isolates was performed using disc-diffusion (Modified-Kirby Baur method) according to CLSIs guidelines. Result: In present study, maximum isolates of Ps. aeruginosa isolated from various samples. The isolates were obtained from different clinical specimens, including pus, urine, respiratory fluids, blood, tissue, and genitalia. -
Supplementary Information Table of Contents Table S1
Supplementary Information Table of Contents Table S1. Matched high-throughput sequencing reads of antibiotic resistance genes (ARGs) in sludge fed with 0 mg/L tetracycline. S1 Table S2. Matched high-throughput sequencing reads of antibiotic resistance genes (ARGs) in sludge fed with 20 mg/L tetracycline. S12 Table S3. Matched high-throughput sequencing reads of plasmids in sludge cultured with 0 mg/L tetracycline. S21 Table S4. Matched high-throughput sequencing reads of plasmids in sludge cultured with 20 mg/L tetracycline. S32 Table S5. PCR primers of the 15 tetracycline resistance genes detected in this study. S40 Figure S1. Occurrence patterns of 11 tet genes in activated sludge analyzed by electrophoresis of PCR products. S41 Table S1. Matched high-throughput sequencing reads of antibiotic resistance genes (ARGs) in sludge fed with 0 mg/L tetracycline of Day 6 against antibiotic resistance database (ARDB). ARDB Accession Identity Hit Length Number ARG No. E Value t Function Related Antibiotics Number (%) n (AA) u of Reads Name 1 CAE53425 90.62 25 7.0 × 10−8 1628 sul2 Sulfonamide-resistant dihydropteroate synthase sulfonamide 2 YP_001969930 90 28 6.0 × 10−9 182 sul2 Sulfonamide-resistant dihydropteroate synthase sulfonamide 3 YP_002112964 100 27 1.0 × 10−11 29 aph33ib Aminoglycoside O-phosphotransferase streptomycin 4 YP_001571041 90 28 5.0 × 10−9 21 macB Macrolide-specific efflux system macrolide 5 YP_002029849 90.32 27 2.0 × 10−8 21 smeE Multidrug resistance efflux pump fluoroquinolone 6 YP_002890644 90.32 31 3.0 × 10−10 21 bacA -
Intracellular Penetration and Effects of Antibiotics On
antibiotics Review Intracellular Penetration and Effects of Antibiotics on Staphylococcus aureus Inside Human Neutrophils: A Comprehensive Review Suzanne Bongers 1 , Pien Hellebrekers 1,2 , Luke P.H. Leenen 1, Leo Koenderman 2,3 and Falco Hietbrink 1,* 1 Department of Surgery, University Medical Center Utrecht, 3508 GA Utrecht, The Netherlands; [email protected] (S.B.); [email protected] (P.H.); [email protected] (L.P.H.L.) 2 Laboratory of Translational Immunology, University Medical Center Utrecht, 3508 GA Utrecht, The Netherlands; [email protected] 3 Department of Pulmonology, University Medical Center Utrecht, 3508 GA Utrecht, The Netherlands * Correspondence: [email protected] Received: 6 April 2019; Accepted: 2 May 2019; Published: 4 May 2019 Abstract: Neutrophils are important assets in defense against invading bacteria like staphylococci. However, (dysfunctioning) neutrophils can also serve as reservoir for pathogens that are able to survive inside the cellular environment. Staphylococcus aureus is a notorious facultative intracellular pathogen. Most vulnerable for neutrophil dysfunction and intracellular infection are immune-deficient patients or, as has recently been described, severely injured patients. These dysfunctional neutrophils can become hide-out spots or “Trojan horses” for S. aureus. This location offers protection to bacteria from most antibiotics and allows transportation of bacteria throughout the body inside moving neutrophils. When neutrophils die, these bacteria are released at different locations. In this review, we therefore focus on the capacity of several groups of antibiotics to enter human neutrophils, kill intracellular S. aureus and affect neutrophil function. We provide an overview of intracellular capacity of available antibiotics to aid in clinical decision making. -
The Antibiotics Composition Comprising Beta-Lactam
(19) & (11) EP 2 062 581 A1 (12) EUROPEAN PATENT APPLICATION published in accordance with Art. 153(4) EPC (43) Date of publication: (51) Int Cl.: 27.05.2009 Bulletin 2009/22 A61K 31/545 (2006.01) A61K 31/546 (2006.01) A61K 31/43 (2006.01) A61K 31/431 (2006.01) (2006.01) (2006.01) (21) Application number: 07785338.0 A61K 31/424 A61K 31/7036 A61K 47/18 (2006.01) A61K 47/12 (2006.01) (2006.01) (2006.01) (22) Date of filing: 14.08.2007 A61K 47/02 A61K 47/04 A61K 9/08 (2006.01) A61K 9/19 (2006.01) A61K 9/72 (2006.01) A61P 31/04 (2006.01) A61P 31/00 (2006.01) (86) International application number: PCT/CN2007/002438 (87) International publication number: WO 2008/025226 (06.03.2008 Gazette 2008/10) (84) Designated Contracting States: (71) Applicant: Tianjin Hemey Bio-Tech Co., Ltd. AT BE BG CH CY CZ DE DK EE ES FI FR GB GR Tianjin 300457 (CN) HU IE IS IT LI LT LU LV MC MT NL PL PT RO SE SI SK TR (72) Inventor: ZHANG, Hesheng Designated Extension States: Tianjin 300457 (CN) AL BA HR MK RS (74) Representative: Hryszkiewicz, Danuta et al (30) Priority: 25.08.2006 CN 200610015437 Kancelaria Patentowa ul. Jana z Kolna 38 PL-75-204 Koszalin (PL) (54) THE ANTIBIOTICS COMPOSITION COMPRISING BETA-LACTAM ANTIBIOTICS AND IONIC CHELATING AGENTS (57) The antibiotics composition comprising at least tors and buffers simultaneously. The composition can be one of beta-lactam antibiotics and at least one of ionic formulated with at least one of aminoglycoside antibiotics chelating agents used for inhibiting particulate formation, into solution for controlling microbial infection in a con- further comprising at least one of beta-lactamase inhib- tainer. -
COMPLETE GENOME SEQUENCING of Pseudomonas Syringae Pv. Actinidiae BIOVAR 3, P155, KIWIFRUIT PATHOGEN ORIGINATING from CHINA SEQU
2220 Bioscience Journal Original Article COMPLETE GENOME SEQUENCING OF Pseudomonas syringae pv. actinidiae BIOVAR 3, P155, KIWIFRUIT PATHOGEN ORIGINATING FROM CHINA SEQUENCIAMENTO COMPLETO DO GENOMA Pseudomonas syringae pv. actinidiae BIOVAR 3, P155, AGENTE PATOGÊNICO DO KIWI, ORIGINÁRIO DA CHINA Xin PAN1,2; Siyue ZHAO3; Yongzhi WANG2; Mingzhang LI2; Liqin HE2*; Qiguo ZHUANG2* 1. College of Tourism and Town and Country Planning, Chengdu University of Technology, Chengdu, Sichuan, China; 2. Kiwifruit Breeding and Utilization Key Laboratory, Sichuan Provincial Academy of Natural Resource Sciences, Chengdu, China; 3. Department of Applied Microbiology, College of Resources, Sichuan Agricultural University, Chengdu, Sichuan, China.*Corresponding author: Qiguo Zhuang, [email protected]; Liqin HE, [email protected] ABSTRACT: Pseudomonas syringae pv. actinidiae is a bacterial pathogen of kiwifruit. Based on the results of the pathogenicity assay, we sequenced the strain Pseudomonas syringae (Psa3) P155 which possesses a series of virulence and resistance genes, CRISPR candidate elements, prophage related sequences, methylation modifications, genomic islands as well as one plasmid. Most importantly, the copper resistance genes copA, copB, copC, copD, and copZ as well as aminoglycoside resistance gene ksgA were identified in strain P155, which would pose a threat to kiwifruit production. The complete sequence we reported here will provide valuable information for a better understanding of the genetic structure and pathogenic characteristics of the genome of P155. KEYWORDS: Actinidia sp. Bacterial canker. Complete sequence. Pathogenicity. Pac-Bio platform. INTRODUCTION the development of whole genome sequencing, virulence and antimicrobial resistance profile of Kiwifruit (Actinidia sp.), an economically bacteria can be predicted. Additionally, the sequence important fruit, is cultivated worldwide for its taste data also provide a level of strain discrimination and and nutritional value (Fujikawa and Sawada 2016). -
List Item Assessment Report for Zinacef
10 September 2012 EMA/CHMP/633654/2012 Assessment report for Zinacef and associated names Pursuant to Article 30 of Directive 2001/83/EC INN : cefuroxime (cefuroxime sodium) Procedure no: EMEA/H/A-30/1158 Assessment Report as adopted by the CHMP with all information of a commercially confidential nature deleted. 7 Westferry Circus ● Canary Wharf ● London E14 4HB ● United Kingdom Telephone +44 (0)20 7418 8400 Facsimile +44 (0)20 7523 7051 E -mail [email protected] Website www.ema.europa.eu An agency of the European Union © European Medicines Agency, 2013. Reproduction is authorised provided the source is acknowledged. Table of contents Table of contents ......................................................................................... 2 1. Background information on the procedure .............................................. 3 1.1. Background information on the basis of the grounds for referral ................................. 3 2.1. Introduction......................................................................................................... 3 2.2. Critical Evaluation ................................................................................................ 4 Section 4.1 - Therapeutic indications ............................................................................. 4 Section 4.2 - Posology and method of administration .................................................... 30 Section 4.3 - Contraindications ................................................................................... 33 Section 4.4 - Special -
Protein Synthesis Inhibitors Lecture Outline
Protein Synthesis Inhibitors • Macrolides - Lincosamides • Aminoglycosides • Tetracyclines • Chloramphenicol • Oxazolidinones • Streptogramins Lecture Outline • Description of protein synthesis - translation • Antibiotics – Structure - function - classification – Mechanism(s) of action – Mechanism(s) of resistance – Spectrum of activity/Indications for use – Pharmacology – Toxicity • Clinical examples 1 Overview of Translation (1) Initiation: • 30S binds RBS of mRNA • AA binds tRNA using aminoacyl-tRNA synthetase • IF2 and fmet-tRNA binds 30S at P site • 50S binds complex 70S resulilting in th e f ormati on of the initiation complex Overview of Translation (2) Initiation – tRNA + AA binds translation elongation factor – Enters ribosome and attaches at the A site 2 Overview of Translation (3) Amino Acid Transfer – Petidyltransferase on 50S ribosome attaches the next AA to the polypeptide – Met added to Leu at A site Overview of Translation (4) Elongation tRNA moved to P site by EF-G creating room at A site for next tRNA Translation termination Occurs at nonsense codon sites e.g. UAA Release factors Ribosome dissociates 3 Mechanisms of Action - Protein Synthesis Inhibitors Macrolides • Broad spectrum antibiotics • Original agent: erythromycin • Azalides: azithromycin and clarithromycin – seltdtiilected antimicrobi bildhal and pharmacoki kitinetic advantages 4 Large 14 member macrolactone ring with one or more deoxy sugars attached. Inhibits formation of 50S ribosome blocking trans- peptidation or translocation. Large 14 member lactone ring