Cysteine to Dehydroalanine 'Or F3-Methyldehydroalanine
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Natural Thiopeptides As a Privileged Scaffold for Drug Discovery and Therapeutic Development
– MEDICINAL Medicinal Chemistry Research (2019) 28:1063 1098 CHEMISTRY https://doi.org/10.1007/s00044-019-02361-1 RESEARCH REVIEW ARTICLE Natural thiopeptides as a privileged scaffold for drug discovery and therapeutic development 1 1 1 1 1 Xiaoqi Shen ● Muhammad Mustafa ● Yanyang Chen ● Yingying Cao ● Jiangtao Gao Received: 6 November 2018 / Accepted: 16 May 2019 / Published online: 29 May 2019 © Springer Science+Business Media, LLC, part of Springer Nature 2019 Abstract Since the start of the 21st century, antibiotic drug discovery and development from natural products has experienced a certain renaissance. Currently, basic scientific research in chemistry and biology of natural products has finally borne fruit for natural product-derived antibiotics drug discovery. A batch of new antibiotic scaffolds were approved for commercial use, including oxazolidinones (linezolid, 2000), lipopeptides (daptomycin, 2003), and mutilins (retapamulin, 2007). Here, we reviewed the thiazolyl peptides (thiopeptides), an ever-expanding family of antibiotics produced by Gram-positive bacteria that have attracted the interest of many research groups thanks to their novel chemical structures and outstanding biological profiles. All members of this family of natural products share their central azole substituted nitrogen-containing six-membered ring and are fi 1234567890();,: 1234567890();,: classi ed into different series. Most of the thiopeptides show nanomolar potencies for a variety of Gram-positive bacterial strains, including methicillin-resistant Staphylococcus aureus (MRSA), vancomycin-resistant enterococci (VRE), and penicillin-resistant Streptococcus pneumonia (PRSP). They also show other interesting properties such as antiplasmodial and anticancer activities. The chemistry and biology of thiopeptides has gathered the attention of many research groups, who have carried out many efforts towards the study of their structure, biological function, and biosynthetic origin. -
Cyanobacterial Peptide Toxins
CYANOBACTERIAL PEPTIDE TOXINS CYANOBACTERIAL PEPTIDE TOXINS 1. Exposure data 1.1 Introduction Cyanobacteria, also known as blue-green algae, are widely distributed in fresh, brackish and marine environments, in soil and on moist surfaces. They are an ancient group of prokaryotic organisms that are found all over the world in environments as diverse as Antarctic soils and volcanic hot springs, often where no other vegetation can exist (Knoll, 2008). Cyanobacteria are considered to be the organisms responsible for the early accumulation of oxygen in the earth’s atmosphere (Knoll, 2008). The name ‘blue- green’ algae derives from the fact that these organisms contain a specific pigment, phycocyanin, which gives many species a slightly blue-green appearance. Cyanobacterial metabolites can be lethally toxic to wildlife, domestic livestock and even humans. Cyanotoxins fall into three broad groups of chemical structure: cyclic peptides, alkaloids and lipopolysaccharides. Table 1.1 gives an overview of the specific toxic substances within these broad groups that are produced by different genera of cyanobacteria together, with their primary target organs in mammals. However, not all cyanobacterial blooms are toxic and neither are all strains within one species. Toxic and non-toxic strains show no predictable difference in appearance and, therefore, physicochemical, biochemical and biological methods are essential for the detection of cyanobacterial toxins. The most frequently reported cyanobacterial toxins are cyclic heptapeptide toxins known as microcystins which can be isolated from several species of the freshwater genera Microcystis , Planktothrix ( Oscillatoria ), Anabaena and Nostoc . More than 70 structural variants of microcystins are known. A structurally very similar class of cyanobacterial toxins is nodularins ( < 10 structural variants), which are cyclic pentapeptide hepatotoxins that are found in the brackish-water cyanobacterium Nodularia . -
NISIN: PRODUCTION and MECHANISM of ANTIMICROBIAL ACTION IJCRR Section: Healthcare Sci
Review Article NISIN: PRODUCTION AND MECHANISM OF ANTIMICROBIAL ACTION IJCRR Section: Healthcare Sci. Journal Impact Factor Sukrita Punyauppa-path, Parichat Phumkhachorn, 4.016 Pongsak Rattanachaikunsopon Department of Biological Science, Faculty of Science, Ubon Ratchathani University, Ubon Ratchathani 34190, Thailand. ABSTRACT Nisin is a heat stable lantibiotic consisting of 34 amino acids. Of these amino acids, there are several unusual amino acids includ- ing dehydroalanine, dehydrobutyrine, aminobutyric acid, lanthionine and β-methyllanthionine. It has antimicrobial activity against many species of Gram positive bacteria, but not Gram negative bacteria due to their outer membrane barriers. However, when used in combination with other chemical or physical treatments that destabilize the outer membranes, nisin can inhibit Gram negative bacteria. Nisin has been used as a food preservative in many food industries because it is legally approved as safe for use in food and beverage. The knowledge on the production and mechanism of antimicrobial action of nisin is important for the understanding how nisin contains unusual amino acids and how it kills sensitive bacteria. The knowledge may also be a factor for the successful application of nisin. Therefore, this review focuses on presenting these two aspects of nisin. Key Words: Bacteriocin, Lactococcus lactis, lanbiotic, nisin INTRODUCTION (Table 1), but not Gram negative bacteria due to their outer membrane barrier. Normally, nisin producer has Nisin is the antimcirobial peptide produced by Lactococ- immunity to its own produced nisin but not to other lan- 1 cus lactis subsp. Lactis . It is the only bacterioicin that tibotics. This is for protecting itself from being killed by have been legally approved as safe for use in food and its own nisin. -
Bacteriotherapy in Breast Cancer
International Journal of Molecular Sciences Review Bacteriotherapy in Breast Cancer 1,2, 3, 4 5 Atieh Yaghoubi y, Majid Khazaei y, Seyed Mahdi Hasanian , Amir Avan , William C. Cho 6,* and Saman Soleimanpour 1,2,* 1 Antimicrobial Resistance Research Center, Bu-Ali Research Institute, Mashhad University of Medical Sciences, Mashhad 91387-35499, Iran; [email protected] 2 Department of Microbiology and Virology, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad 91387-35499, Iran 3 Department of Physiology, Faculty of Medicine, Mashhad University of Medical Sciences, Mashhad 9138735499, Iran; [email protected] 4 Department of Medical Biochemistry, Faculty of Medicine, Mashhad University of Medical, Sciences, Mashhad 91387-35499, Iran; [email protected] 5 Cancer Research Center, Mashhad University of Medical Sciences, Mashhad 91387-35499, Iran; [email protected] 6 Department of Clinical Oncology, Queen Elizabeth Hospital, Kowloon, Hong Kong * Correspondence: [email protected] or [email protected] (W.C.C.); [email protected] (S.S.); Tel.: +852-3506-6284 (W.C.C.); +98-912-6590-092 (S.S.); Fax: +852-3506-5455 (W.C.C.); +98-511-8409-612 (S.S.) These authors contributed equally to this work. y Received: 2 October 2019; Accepted: 18 November 2019; Published: 23 November 2019 Abstract: Breast cancer is the second most common cause of cancer-related mortality among women around the world. Conventional treatments in the fight against breast cancer, such as chemotherapy, are being challenged regarding their effectiveness. Thus, strategies for the treatment of breast cancer need to be continuously refined to achieve a better patient outcome. -
First Evidence of Production of the Lantibiotic Nisin P Enriqueta Garcia-Gutierrez1,2, Paula M
www.nature.com/scientificreports OPEN First evidence of production of the lantibiotic nisin P Enriqueta Garcia-Gutierrez1,2, Paula M. O’Connor2,3, Gerhard Saalbach4, Calum J. Walsh2,3, James W. Hegarty2,3, Caitriona M. Guinane2,5, Melinda J. Mayer1, Arjan Narbad1* & Paul D. Cotter2,3 Nisin P is a natural nisin variant, the genetic determinants for which were previously identifed in the genomes of two Streptococcus species, albeit with no confrmed evidence of production. Here we describe Streptococcus agalactiae DPC7040, a human faecal isolate, which exhibits antimicrobial activity against a panel of gut and food isolates by virtue of producing nisin P. Nisin P was purifed, and its predicted structure was confrmed by nanoLC-MS/MS, with both the fully modifed peptide and a variant without rings B and E being identifed. Additionally, we compared its spectrum of inhibition and minimum inhibitory concentration (MIC) with that of nisin A and its antimicrobial efect in a faecal fermentation in comparison with nisin A and H. We found that its antimicrobial activity was less potent than nisin A and H, and we propose a link between this reduced activity and the peptide structure. Nisin is a small peptide with antimicrobial activity against a wide range of pathogenic bacteria. It was originally sourced from a Lactococcus lactis subsp. lactis isolated from a dairy product1 and is classifed as a class I bacteri- ocin, as it is ribosomally synthesised and post-translationally modifed2. Nisin has been studied extensively and has a wide range of applications in the food industry, biomedicine, veterinary and research felds3–6. -
Functional Interaction of Human Neutrophil Peptide-1 with the Cell Wall Precursor Lipid II
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 584 (2010) 1543–1548 journal homepage: www.FEBSLetters.org Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II Erik de Leeuw a,*, Changqing Li a, Pengyun Zeng b, Chong Li b, Marlies Diepeveen-de Buin c, Wei-Yue Lu b, Eefjan Breukink c, Wuyuan Lu a,** a University of Maryland Baltimore School of Medicine, Institute of Human Virology and Department of Biochemistry and Molecular Biology, 725 West Lombard Street, Baltimore, MD 21201, USA b Fudan University School of Pharmacy, Shanghai, China c Utrecht University, Department of Biochemistry of Membranes, Bijvoet Center for Biomolecular Research, Padualaan 8, 3585 CH, Utrecht, The Netherlands article info abstract Article history: Defensins constitute a major class of cationic antimicrobial peptides in mammals and vertebrates, Received 11 January 2010 acting as effectors of innate immunity against infectious microorganisms. It is generally accepted Revised 1 March 2010 that defensins are bactericidal by disrupting the anionic microbial membrane. Here, we provide evi- Accepted 2 March 2010 dence that membrane activity of human a-defensins does not correlate with antibacterial killing. Available online 7 March 2010 We further show that the a-defensin human neutrophil peptide-1 (HNP1) binds to the cell wall pre- Edited by Renee Tsolis cursor lipid II and that reduction of lipid II levels in the bacterial membrane significantly reduces bacterial killing. The interaction between defensins and lipid II suggests the inhibition of cell wall synthesis as a novel antibacterial mechanism of this important class of host defense peptides. -
UC San Diego UC San Diego Electronic Theses and Dissertations
UC San Diego UC San Diego Electronic Theses and Dissertations Title Probiogenomic Analysis of Three Commonly Occuring Bifidobacterial Species Permalink https://escholarship.org/uc/item/8d67d715 Author Kim, Andrew Min Publication Date 2018 Peer reviewed|Thesis/dissertation eScholarship.org Powered by the California Digital Library University of California UNIVERSITY OF CALIFORNIA SAN DIEGO Probiogenomic Analysis of Three Commonly Occuring Bifidobacterial Species A Thesis submitted in partial satisfaction of the requirements for the degree Master of Science in Biology by Andrew Min Kim Committee in charge: Milton Saier, Chair Eric Allen, Co-Chair Stanley Lo 2018 © Copyright Andrew Min Kim, 2018 All rights reserved. The Thesis of Andrew Min Kim is approved, and it is acceptable in quality and form for publication on microfilm and electronically: Co-Chair Chair University of California San Diego 2018 iii TABLE OF CONTENTS Signature Page ........................................................................................................... iii Table of Contents ....................................................................................................... iv List of Tables ............................................................................................................. v Acknowledgements .................................................................................................... vi Abstract of the Thesis ................................................................................................ vii Introduction -
Antibacterial Effect of High-Purity Nisin Alone and in Combination with D-Amino Acids Or Chlorhexidine in an Endodontic-Like Biofilm Model
antibiotics Article Antibacterial Effect of High-Purity Nisin Alone and in Combination with D-Amino Acids or Chlorhexidine in an Endodontic-Like Biofilm Model Ericka T. Pinheiro 1,2,* , Lamprini Karygianni 2 , Thomas Attin 2 and Thomas Thurnheer 2 1 Department of Dentistry, School of Dentistry, University of São Paulo, São Paulo 01000-000, Brazil 2 Clinic of Conservative and Preventive Dentistry, Center of Dental Medicine, University of Zurich, CH-8032 Zürich, Switzerland; [email protected] (L.K.); [email protected] (T.A.); [email protected] (T.T.) * Correspondence: [email protected] or [email protected]; Tel.: +41-44-634-32-56 Abstract: New strategies to eradicate endodontic biofilms are needed. Therefore, we evaluated the effect of high-purity nisin alone and in combination with D-amino acids (D-AAs) or chlorhexidine (CHX) against an “endodontic-like” biofilm model. Biofilms were grown on hydroxyapatite discs for 64 h and treated with nisin, eight D-AAs mixture, nisin + eight D-AAs, 2% CHX, and nisin + 2% CHX. After the 5 min and 24 h treatments, biofilm cells were harvested and total colony-forming units were counted. Differences between groups were tested by two-way ANOVA followed by Tukey’s multiple comparisons test (p < 0.05). Nisin and D-AAs, alone or in combination, were not effective in reducing bacteria after short or long exposure times. After 5 min, treatment with 2% CHX and nisin + 2% CHX resulted in 2 and 2.4-log cell reduction, respectively, compared with the no treatment control (p < 0.001). -
NISIN and the MARKET for COMMERICIAL BACTERIOCINS Dr
NISIN AND THE MARKET FOR COMMERICIAL BACTERIOCINS Dr. Eluned Jones Dr. Victoria Salin Dr. Gary W. Williams* TAMRC Consumer and Product Research Report No. CP-01-05 July 2005 * Jones and Salin are Associate Professors and Williams is Professor of Agricultural Economics and Director, Texas Agricultural Market Research, Department of Agricultural Economics, Texas A&M University, College Station, Texas 77843-2124. NISIN AND THE MARKET FOR COMMERICIAL BACTERIOCINS Texas Agribusiness Market Research Center (TAMRC) Consumer and Product Research Report No. CP-01-05 by Dr. Eluned Jones, Dr. Victoria Salin, and Dr. Gary W. Williams, July 2005. Abstract: This report provides a background analysis of the market for nisin and other commercially available antimicrobial food additives. The report concludes that there is a potential role for a new U.S.-based entity to compete with a nisin product that is cost-competitive or provides quality guarantees to satisfy U.S. buyers who have tight specifications for ingredient sourcing and food safety and quality oversight. Acknowledgements The research reported here was conducted under contract for the National Corn Growers Association (NCGA). Thanks are due to Richard Glass and Nathan Fields of the NCGA for their support. The conclusions reached and any views expressed, however, are those of the authors and may not represent those of NCGA or of Texas A&M University. The Texas Agribusiness Market Research Center (TAMRC) has been providing timely, unique, and professional research on a wide range of issues relating to agricultural and agribusiness markets and products of importance to Texas and the nation for thirty-five years. -
Thelactococcus Lactis Nisin-Sucrose Conjugative Transposon Tti5276
The Lactococcus lactis Nisin-Sucrose Conjugative Transposon Tti5276 0000 0513475 0 [: ijC, $ Promoter: dr. W. M. deVo s hoogleraar in de bacteriele genetica 3 fjrj 02?€>\ ^ f Peter Jacobus GerardusRauc h The Lactococcus lactisNisin-Sucros e Conjugative Transposon Tn5276 Proefschrift ter verkrijging van de graad van doctor in de landbouw- enmilieuwetenschappe n op gezag van de rector magnificus dr. H. C. van der Plas, in het openbaar te verdedigen op woensdag 26 mei 1993 des namiddags te vier uur in de Aula van de Landbouwuniversiteit te Wageningen \^v \ ; ^ "A% -^ c\ \ J De natuur is beweging. James Hutton Tendage dat ikriep, hebtGij mi) geantwoord, Gijhebt mi) bemoedigd metkracht in mijn ziel. Psalm 138(NB G vertaling) BIBLIOTHEER OSNDBOUWUNIVEBSOBW SPAGENlNGEtt Aan papen mam, Catelijne, Marijke en Lonneke ] I-JI y)3X> i STELLINGEN 1. Debewerin gva nPoyart-Salmero n etal. datd eplaats-specifiek e recombinatie-reactie van Tnl545 zich onderscheidt van die van bacteriofaag Xdoorda t het Int-Tn eiwit ook functioneert in afwezigheid van Xis-Tn is onjuist. Poyart-Salmeron, C, P. Trieu-Cuot, C. Carlier en P. Courvalin. 1989. Molecular characterization of twoprotein s involved inth e excision ofth e conjugative transposon Tnl545: homologies with other site-specific recombinases. EMBOJ . 8:2425-2433. Abremski, K. enS. Gottesman. 1981. Site-specific recombination. Xis-independent excisive recombination of bacteriophage lambda. J. Mol. Biol. 153:67-78. De bewering van Steen et al. dat het structurele nisine gen van Lactococcus lactis ATCC 11454 afgeschreven wordt vanuit een promoter die meer dan 4 kb stroomopwaarts ligt, is onwaarschijnlijk aangezien transcriptie van dit gen dan afhankelijk zou zijn van de plaats van insertie van het nisine-sucrose element in het chromosoom en van mogelijke IS-gemedieerde herrangschikkingen van het gebied tussen het startpunt van transcriptie en het nisine gen. -
University of Groningen Invitro Pore-Forming Activity of The
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by University of Groningen University of Groningen Invitro pore-forming activity of the lantibiotic nisin - role of protonmotive force and lipid- composition Garcia Garcera, Maria J.; Elferink, Marieke G. L.; Driessen, Arnold J. M.; Konings, Wil N. Published in: European Journal of Biochemistry DOI: 10.1111/j.1432-1033.1993.tb17677.x IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 1993 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Garcia Garcera, M. J., Elferink, M. G. L., Driessen, A. J. M., & Konings, W. N. (1993). Invitro pore-forming activity of the lantibiotic nisin - role of protonmotive force and lipid-composition. European Journal of Biochemistry, 212(2), 417-422. https://doi.org/10.1111/j.1432-1033.1993.tb17677.x Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. -
Enzyme Annotation for Orphan and Novel Reactions Using Knowledge of Substrate Reactive Sites
Enzyme annotation for orphan and novel reactions using knowledge of substrate reactive sites Noushin Hadadia,1, Homa MohammadiPeyhania,1, Ljubisa Miskovica, Marianne Seijoa,2, and Vassily Hatzimanikatisa,3 aLaboratory of Computational Systems Biology, Institute of Chemistry and Chemical Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland Edited by Sang Yup Lee, Korea Advanced Institute of Science and Technology, Daejeon, South Korea, and approved March 6, 2019 (received for review November 5, 2018) Thousands of biochemical reactions with characterized activities metabolic engineering, synthetic biology applications, and the gap are “orphan,” meaning they cannot be assigned to a specific enzyme, filling of genome-scale models (19). A method for associating de leaving gaps in metabolic pathways. Novel reactions predicted by novo reactions to similarly occurring natural enzymatic reactions pathway-generation tools also lack associated sequences, limiting would allow for the direct experimental implementation of the protein engineering applications. Associating orphan and novel discovered novel reactions or assist in designing new proteins capable reactions with known biochemistry and suggesting enzymes to of catalyzing the proposed biotransformation. catalyze them is a daunting problem. We propose the method BridgIT Computational methods for identifying candidate genes of to identify candidate genes and catalyzing proteins for these re- orphan reactions have mostly been developed on the basis on actions. This method introduces information about the enzyme protein sequence similarity (3, 20–22). The two predominant binding pocket into reaction-similarity comparisons. BridgIT assesses classes of these sequence-based methods revolve around gene/ the similarity of two reactions, one orphan and one well-characterized genome analysis (22–25) and metabolic information (26, 27).