Conferencebookletfinal.Pdf
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Effect of Soybean Oligopeptide on the Growth and Metabolism Of
RSC Advances View Article Online PAPER View Journal | View Issue Effect of soybean oligopeptide on the growth and metabolism of Lactobacillus acidophilus JCM 1132 Cite this: RSC Adv., 2020, 10,16737 Wenhui Li, Yinxiao Zhang, He Li, * Chi Zhang, Jian Zhang, Jalal Uddin and Xinqi Liu* Soybean protein (Pro) and soybean oligopeptide (Pep) were subjected to simulated digestion in vitro to study the effect of Pep on the growth and metabolism of Lactobacillus acidophilus JCM 1132. First, the molecular weight distribution differences of samples before and after digestion were compared, and the samples were used to replace the nitrogen source components in the culture media. Then, the viable cell numbers, lactic acid and acetic acid content, differential metabolites, and metabolic pathways during the culturing process were measured. Results showed that the digested soybean oligopeptide (dPep) was less efficient than MRS medium in promoting the growth, but by increasing the content of the intermediates during the tricarboxylic acid (TCA) cycle, its metabolic capacity was significantly improved. Received 20th February 2020 Besides, due to the low molecular weight of dPep, it can be better transported and utilized. And dPep Creative Commons Attribution 3.0 Unported Licence. Accepted 20th April 2020 significantly strengthened the amino acid metabolism and weakened the glycerol phospholipid DOI: 10.1039/d0ra01632b metabolism, so the ability of dPep in promoting the growth and metabolism of Lactobacillus acidophilus rsc.li/rsc-advances JCM 1132 is higher than the digested soybean protein (dPro). 1. Introduction represent those that reach the intestine and directly acts on the intestinal ora aer digestion by the human body.13,14 Although Pro is a high-quality, nutritionally balanced plant Probiotics are mainly composed of Lactobacillus and Bido- protein displaying an excellent amino acid composition, it has bacterium. -
Terminology of Bioanalytical Methods (IUPAC Recommendations 2018) Received November 21, 2016; Accepted February 1, 2018
Pure Appl. Chem. 2018; 90(7): 1121–1198 IUPAC Recommendations Ján Labuda, Richard P. Bowater, Miroslav Fojta, Günter Gauglitz, Zdeněk Glatz, Ivan Hapala, Jan Havliš, Ferenc Kilar, Aniko Kilar, Lenka Malinovská, Heli M. M. Sirén, Petr Skládal, Federico Torta, Martin Valachovič, Michaela Wimmerová, Zbyněk Zdráhal and David Brynn Hibbert* Terminology of bioanalytical methods (IUPAC Recommendations 2018) https://doi.org/10.1515/pac-2016-1120 Received November 21, 2016; accepted February 1, 2018 Abstract: Recommendations are given concerning the terminology of methods of bioanalytical chemistry. With respect to dynamic development particularly in the analysis and investigation of biomacromolecules, terms related to bioanalytical samples, enzymatic methods, immunoanalytical methods, methods used in genomics and nucleic acid analysis, proteomics, metabolomics, glycomics, lipidomics, and biomolecules interaction studies are introduced. Keywords: bioanalytical samples; biomolecule interaction studies; enzymatic methods; genomics; glycom- ics; immunoanalytical methods; lipidomics; metabolomics; nucleic acid analysis; proteomics. CONTENTS 1. PREFACE �������������������������������������������������������������������������������������������������������������������������������������� 1122 2. INTRODUCTION ��������������������������������������������������������������������������������������������������������������������������� 1122 3. BIOANALYTICAL SAMPLES ���������������������������������������������������������������������������������������������������������� -
Genscript Product Catalog 2013-2014 Genscript Product Catalog
GenScript Product Catalog 2013-2014 GenScript Product Catalog www.genscript.com GenScript USA Inc. 860 Centennial Ave. Piscataway, NJ 08854USA Tel: 1-732-885-9188 / 1-732-885-9688 Toll-Free Tel: 1-877-436-7274 Fax: 1-732-210-0262 / 1-732-885-5878 Email: [email protected] Nucleic Acid Purification and Analysis Business Development Tel: 1-732-317-5088 PCR PCR and Cloning Email: [email protected] Protein Analysis Antibodies 2013-2014 Peptides Welcome to GenScript GenScript USA Incorporation, founded in 2002, is a fast-growing biotechnology company and contract research organization (CRO) specialized in custom services and consumable products for academic and pharmaceutical research. Built on our assembly-line mode, one-stop solutions, continuous improvement, and stringent IP protection, GenScript provides a comprehensive portfolio of products and services at the most competitive prices in the industry to meet your research needs every day. Over the years, GenScript’s scientists have developed many innovative technologies that allow us to maintain our position at the cutting edge of biological and medical research while offering cost-effective solutions for customers to accelerate their research. Our advanced expertise includes proprietary technology for custom gene synthesis, OptimumGeneTM codon optimization technology, CloneEZ® seamless cloning technology, FlexPeptideTM technology for custom peptide synthesis, BacPowerTM technology for protein expression and purification, T-MaxTM adjuvant and advanced nanotechnology for custom antibody production, as well as our ONE-HOUR WesternTM detection system and eStain® protein staining system. GenScript offers a broad range of reagents, optimized kits, and system solutions to help you unravel the mysteries of biology. We also provide a comprehensive portfolio of customized services that include Bio-Reagent, Bio-Assay, Lead Optimization, and Antibody Drug Development which can be effectively integrated into your value chain and your operations. -
Applications of Oligopeptide-Functionalized
APPLICATIONS OF OLIGOPEPTIDE-FUNCTIONALIZED SURFACES AND MICROPARTICLES IN LIQUID CRYSTALS- BASED ASSAYS ONG LIAN HAO (B.ENG. (HONS.), NANYANG TECHNOLOGICAL UNIVERSITY) A THESIS SUBMITTED FOR THE DEGREE OF DOCTOR OF PHILOSOPHY DEPARTMENT OF CHEMICAL AND BIOMOLECULAR ENGINEERING NATIONAL UNIVERSITY OF SINGAPORE 2016 DECLARATION I hereby declare that this thesis is my original work and it has been written by me in its entirety. I have duly acknowledged all the sources of information which have been used in the thesis. This thesis has also not been submitted for any degree in any university previously. Ong Lian Hao 10 September 2016 i ACKNOWLEDGEMENTS First of all, I am utmost grateful for the opportunity presented by my advisor, Dr. Yang Kun-Lin, to complete this thesis under his guidance. His insightful perspectives and open-door policy provided a conducive environment for me to develop and hone my research skills and ideologies. I am also thankful for the engaging, and more importantly enlightening discussions with our group members, and they include Dr. Liu Fengli, Dr. Chen Chih-Hsin, Dr. Ding Xiaokang, Ms. Liu Yanyang, Ms. Nguyen Le Truc and Dr. Arumugam Kamayan Rajagopalan G. I am also fortunate to receive guidance and advice from Dr. Saif Khan and his group members during our regular intergroup sharing sessions. I would also like to thank the friendly laboratory staff for their assistance in the procurement and operation of equipment, and they include Mr. Boey Kok Hong, Ms. Lee Chai Keng, Mr. Liu Zhicheng, Ms. Lim Kwee Mei, Dr. Yuan Ze Liang and Dr. Yang Liming. Finally, I am grateful to my parents and parents-in-law for their support. -
(12) United States Patent (10) Patent No.: US 9,353,350 B2 Kobayashi Et Al
US009353350B2 (12) United States Patent (10) Patent No.: US 9,353,350 B2 Kobayashi et al. (45) Date of Patent: May 31, 2016 (54) METHOD FOR PRODUCING MULTIPOLAR 2012fO149053 A1 6, 2012 Yoshida et al. CELL 2013,0323,776 A1 12/2013 Yoshida et al. 2015. OO18286 A1* 1/2015 Kobayashi et al. .......... 514, 19.3 (71) Applicant: TOAGOSEICO.,LTD., Tokyo (JP) FOREIGN PATENT DOCUMENTS (72) Inventors: Nahoko Kobayashi, Tsukuba (JP); CN 1763O82 A 4/2006 Tetsuhiko Yoshida, Tsukuba (JP); Yuki DE 102009021681 A1 11, 2010 Kobayashi, Fujisawa (JP) WO O3O24408 A2 3, 2003 WO O3O37172 A2 5, 2003 WO 2004.005472 A2 1, 2004 (73) Assignee: TOAGOSEICO. LTD., Tokyo (JP) WO 2004/020457 A2 3, 2004 WO 2007/004869 A2 1, 2007 (*) Notice: Subject to any disclaimer, the term of this WO 2007056188 A1 5/2007 patent is extended or adjusted under 35 WO 2008/081812 A1 T 2008 WO WO 2009,093692 A1 T 2009 U.S.C. 154(b) by 0 days. WO WO 2011/O13698 A1 2, 2011 (21) Appl. No.: 14/366,971 WO WO 2011/O13699 A1 2, 2011 (22) PCT Filed: Dec. 20, 2012 OTHER PUBLICATIONS Paradis-Bleau et al., “Peptide inhibitors of the essential cell division (86). PCT No.: PCT/UP2O12AO83110 protein FtsA'. Protein Engineering, Design & Selection, 2005, pp. S371 (c)(1), 85-91, vol. 18, No. 2, Oxford University Press. (2) Date: Jun. 19, 2014 Paradis-Bleau et al., “Identification of Pseudomonas aeruginosa FtsZ. peptide inhibitors as a tool for development of novel antimicro bials”, Journal of Antimicrobial Chemotherapy, Jun. 2004, pp. -
Synthesis of Equimolar Multiple Oligomer Mixtures
Europaisches Patentamt (19) European Patent Office Office europeenpeen des brevets EP 0 558 671 B1 (12) EUROPEAN PATENT SPECIFICATION (45) Date of publication and mention (51) intci.6: C07K1/04, C07K7/06, of the grant of the patent: A61 K 38/00, G01 N 33/53 27.01.1999 Bulletin 1999/04 (86) International application number: (21) Application number: 92902209.3 PCT/US91/08694 Date of 20.11.1991 (22) filing: (87) International publication number: WO 92/09300 (11.06.1992 Gazette 1992/13) (54) SYNTHESIS OF EQUIMOLAR MULTIPLE OLIGOMER MIXTURES, ESPECIALLY OF OLIGOPEPTIDE MIXTURES SYNTHESE AQUIMOLARER MISCHUNGEN VIELZAHLIGER OLIGOMERE, SPEZIELL OLIGOPEPTIDMISCHUNGEN SYNTHESE DE MELANGES OLIGOMERES MULTIPLES EQUIMOLAIRES, NOTAMMENT DE MELANGES D'OLIGOPEPTIDES (84) Designated Contracting States: (56) References cited: AT BE CH DE DK ES FR GB GR IT LI LU NL SE US-A- 4 631 211 US-A-5 010 175 (30) Priority: 21.11.1990 US 617023 BANBURY REP. vol. 29, 1988, pages 151-161 16.05.1991 US 701658 HOUGHTEN, R.A. 'Exact amino acid involvement 19.11.1991 US 797551 in the interactions of peptide antigens with monoclonal antibodies' (43) Date of publication of application: PROTIDES BIOL. FLUIDS vol. 34, 1986, pages 19 08.09.1993 Bulletin 1993/36 - 22 HOUGHTEN, R.A. 'Facile determination of exact amino acid involvement in peptide (73) Proprietor: ITEREX PHARMACEUTICALS LTD. antigen/monoclonal antibody interactions' PARTNERSHIP J. IMMUNOL, vol. 144, no. 3, 1 February 1990, San Diego, C A 92121 (US) pages 976 - 983 APPEL J.R. ET AL. 'Elucidation of discontinuous linear determinants in (72) Inventors: peptides' • HOUGHTEN, Richard, A. -
Amide Bond Formation in Nonribosomal Peptide Synthesis
Amide Bond Formation in Nonribosomal Peptide Synthesis: The Formylation and Condensation Domains Dissertation zur Erlangung des Doktorgrades der Naturwissenschaften (Dr. rer. nat.) dem Fachbereich Chemie der Philipps-Universität Marburg vorgelegt von Georg Schönafinger aus München Marburg/Lahn 2007 Vom Fachbereich Chemie der Philipps-Universität Marburg als Dissertation am _______________ angenommen. Erstgutachter : Prof. Dr. M. A. Marahiel (Philipps-Universität, Marburg) Zweitgutachter : Prof. Dr. L.-O. Essen (Philipps-Universität, Marburg) Tag der Disputation: 20. Dezember 2007 2 The majority of the work presented here has been published: Samel, S.A.†, Schoenafinger, G. †, Knappe, T.A., Marahiel, M.A., Essen, L.O. 2007. Structural and functional insights into a peptide bond-forming bidomain from a nonribosomal peptide synthetase. Structure 15(7): 781-92. † equal contribution Schoenafinger, G., Schracke, N., Linne, U., Marahiel, M.A. 2006. Formylation domain: an essential modifying enzyme for the nonribosomal biosynthesis of linear gramicidin. J Am Chem Soc. 128(23): 7406-7. Schoenafinger, G., Marahiel, M.A. accepted 2007. Nonribosomal Peptides. Wiley Encyclopaedia of Chemical Biology. In press. 3 To Anke 4 Summary Nonribosomal peptides are of outstanding pharmacological interest, since many representatives of this highly diverse class of natural products exhibit therapeutically important activities, such as antibacterial, antitumor and immunosuppressive properties. Understanding their biosynthesis performed by multimodular mega-enzymes, the nonribosomal peptide synthetases (NRPSs), is one of the key determinants in order to be able to reprogram these machineries for the production of novel therapeutics. The central structural motif of all peptides is the peptide (or amide) bond. In this work, two different amide bond forming catalytic entities from NRPSs were studied: The condensation (C) and formylation (F) domains. -
A Simplified Reconstitution of Mrna-Directed Peptide Synthesis: Activity of the Epsilon Enhancer and an Unnatural Amino Acid1
Analytical Biochemistry 297, 60–70 (2001) doi:10.1006/abio.2001.5329, available online at http://www.idealibrary.com on A Simplified Reconstitution of mRNA-Directed Peptide Synthesis: Activity of the Epsilon Enhancer and an Unnatural Amino Acid1 Anthony C. Forster,*,2 Herbert Weissbach,† and Stephen C. Blacklow*,2 *Department of Pathology, Brigham and Women’s Hospital and Harvard Medical School, 75 Francis Street, Boston, Massachusetts 02115; and †Center for Molecular Biology and Biotechnology, Florida Atlantic University, 777 Glades Road, Boca Raton, Florida 33431 Received March 13, 2001; published online August 30, 2001 Key Words: translation; reconstitution; E. coli; ribo- The study of the early events in translation would some; initiation factor; elongation factor; tRNA; en- be greatly facilitated by reconstitution with easily hancer; epsilon; peptide; unnatural amino acid; biotin. purified components. Here, Escherichia coli oli- gopeptide synthesis has been reconstituted using five purified recombinant His-tagged E. coli initia- tion and elongation factors. Highly purified ribo- The initiation of translation is a major control point somes are required to yield products with strong in gene expression and is the target of a number of dependencies on the translation factors. Based on cytotoxic agents (1). Initiation is less well understood HPLC separation of radiolabeled translation prod- than elongation and termination in eubacteria (2–4), ucts from an mRNA encoding a tetrapeptide, approx- and initiation is much more complex in eukaryotes (5). imately 80% of peptide products are full length, and It therefore seems likely that the study of the simpler the remaining 20% are the dipeptide and tripeptide eubacterial initiation process may be helpful both in products resulting from pausing or premature ter- the elucidation of general mechanistic principles em- mination. -
A Global Review on Short Peptides: Frontiers and Perspectives †
molecules Review A Global Review on Short Peptides: Frontiers and Perspectives † Vasso Apostolopoulos 1 , Joanna Bojarska 2,* , Tsun-Thai Chai 3 , Sherif Elnagdy 4 , Krzysztof Kaczmarek 5 , John Matsoukas 1,6,7, Roger New 8,9, Keykavous Parang 10 , Octavio Paredes Lopez 11 , Hamideh Parhiz 12, Conrad O. Perera 13, Monica Pickholz 14,15, Milan Remko 16, Michele Saviano 17, Mariusz Skwarczynski 18, Yefeng Tang 19, Wojciech M. Wolf 2,*, Taku Yoshiya 20 , Janusz Zabrocki 5, Piotr Zielenkiewicz 21,22 , Maha AlKhazindar 4 , Vanessa Barriga 1, Konstantinos Kelaidonis 6, Elham Mousavinezhad Sarasia 9 and Istvan Toth 18,23,24 1 Institute for Health and Sport, Victoria University, Melbourne, VIC 3030, Australia; [email protected] (V.A.); [email protected] (J.M.); [email protected] (V.B.) 2 Institute of General and Ecological Chemistry, Faculty of Chemistry, Lodz University of Technology, Zeromskiego˙ 116, 90-924 Lodz, Poland 3 Department of Chemical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Kampar 31900, Malaysia; [email protected] 4 Botany and Microbiology Department, Faculty of Science, Cairo University, Gamaa St., Giza 12613, Egypt; [email protected] (S.E.); [email protected] (M.A.) 5 Institute of Organic Chemistry, Faculty of Chemistry, Lodz University of Technology, Zeromskiego˙ 116, 90-924 Lodz, Poland; [email protected] (K.K.); [email protected] (J.Z.) 6 NewDrug, Patras Science Park, 26500 Patras, Greece; [email protected] 7 Department of Physiology and Pharmacology, -
Safety Assessment of Tripeptide-1, Hexapeptide-12, and Related Amides As Used in Cosmetics
Safety Assessment of Tripeptide-1, Hexapeptide-12, and Related Amides as Used in Cosmetics Status: Draft Report for Panel Review Release Date: February 21, 2014 Panel Meeting Date: March 17-18, 2014 The 2014 Cosmetic Ingredient Review Expert Panel members are: Chair, Wilma F. Bergfeld, M.D., F.A.C.P.; Donald V. Belsito, M.D.; Curtis D. Klaassen, Ph.D.; Daniel C. Liebler, Ph.D.; Ronald A Hill, Ph.D. James G. Marks, Jr., M.D.; Ronald C. Shank, Ph.D.; Thomas J. Slaga, Ph.D.; and Paul W. Snyder, D.V.M., Ph.D. The CIR Director is Lillian J. Gill, D.P.A. This report was prepared by Wilbur Johnson, Jr., M.S., Senior Scientific Analyst and Bart Heldreth, Ph.D., Chemist. © Cosmetic Ingredient Review 1620 L STREET, N.W., SUITE 1200 ◊ WASHINGTON, DC 20036-4702 ◊ PH 202.331.0651 ◊ FAX 202.331.0088 ◊ [email protected] Commitment & Credibility since 1976 Memorandum To: CIR Expert Panel Members and Liaisons From: Wilbur Johnson, Jr. Senior Scientific Analyst Date: February 21, 2014 Subject: Draft Report on Tripeptide-1, Hexapeptide-12, and Related Amides The draft report on palmitoyl oligopeptides was tabled at the March 18-19, 2013 CIR Expert Panel meeting, pending reorganization of the safety assessment. During the meeting, the Panel was provided with a letter from the CIR Science and Support Committee, recommending the creation of a new ingredient group consisting of ingredients for which the peptide sequence is known, namely, tripeptide -1, hexapeptide-12 and specific related amides. This has been done. Additionally, at the March meeting, further information was sought to better understand the extent and manner in which solid-phase peptide synthesis is used to create the peptide portion of ingredients included in the safety assessment. -
Diversity of Peptides Produced by Nodularia Spumigena from Various Geographical Regions
Mar. Drugs 2013, 11, 1-19; doi:10.3390/md11010001 OPEN ACCESS Marine Drugs ISSN 1660-3397 www.mdpi.com/journal/marinedrugs Article Diversity of Peptides Produced by Nodularia spumigena from Various Geographical Regions Hanna Mazur-Marzec 1,*, Monika J. Kaczkowska 1, Agata Blaszczyk 1, Reyhan Akcaalan 2, Lisa Spoof 3 and Jussi Meriluoto 3 1 Department of Marine Biology and Ecology, University of Gdansk, Al. Marszałka Piłsudskiego 46, Gdynia 81-378, Poland; E-Mails: [email protected] (M.J.K.); [email protected] (A.B.) 2 Faculty of Fisheries, Istanbul University, Ordu Cad. No. 200, 34470 Laleli, Istanbul, Turkey; E-Mail: [email protected] 3 Department of Biosciences, Abo Akademi University, Tykistök atu 6A, Turku 20520, Finland; E-Mails: [email protected] (L.S.); [email protected] (J.M.) * Author to whom correspondence should be addressed; E-Mail: [email protected]; Tel.: +48-58-523-6621; Fax: +48-58-523-6712. Received: 12 October 2012; in revised form: 13 November 2012 / Accepted: 11 December 2012 / Published: 21 December 2012 Abstract: Cyanobacteria produce a great variety of non-ribosomal peptides. Among these compounds, both acute toxins and potential drug candidates have been reported. The profile of the peptides, as a stable and specific feature of an individual strain, can be used to discriminate cyanobacteria at sub-population levels. In our work, liquid chromatography-tandem mass spectrometry was used to elucidate the structures of non-ribosomal peptides produced by Nodularia spumigena from the Baltic Sea, the coastal waters of southern Australia and Lake Iznik in Turkey. -
New Biodegradable Peptide-Based Polymer Constructs
New Biodegradable Peptide-based Polymer Constructs Maarten van Dijk New Biodegradable Peptide-based Polymer Constructs Maarten van Dijk PhD thesis with summary in Dutch Department of Medicinal Chemistry and Chemical Biology and Department of Pharmaceutics, Utrecht University, Utrecht, The Netherlands October 2009 ISBN: 978-90-393-5165-9 © 2009 by Maarten van Dijk. All rights reserved. No part of this thesis may be reproduced or transmitted in any form or by any means, without written permission from the author. New Biodegradable Peptide-based Polymer Constructs Nieuwe biodegradeerbare polymeerconstructen gebaseerd op peptiden (met een samenvatting in het Nederlands) Proefschrift ter verkrijging van de graad van doctor aan de Universiteit Utrecht op gezag van de rector magnificus, prof.dr. J.C. Stoof, ingevolge het besluit van het college voor promoties in het openbaar te verdedigen op maandag 5 oktober 2009 des middags te 4.15 uur door Maarten van Dijk geboren op 3 maart 1980 te Rotterdam Promotoren: Prof. dr. R.M.J. Liskamp Prof. dr. ir. W.E. Hennink Co-promotoren: Dr. ir. D.T.S. Rijkers Dr. C.F. van Nostrum Contents Chapter 1 General Introduction 7 Chapter 2 Synthesis and Applications of Biomedical and 19 Pharmaceutical Polymers via Click Chemistry Methodologies Chapter 3 Synthesis of Peptide-based Polymers by 51 Microwave-assisted Cycloaddition Backbone Polymerization Chapter 4 Synthesis and Characterization of Biodegradable 73 Peptide-based Polymers Prepared by Microwave- assisted Click Chemistry Chapter 5 Synthesis and Characterization