Prof. Dr. Jörg Andrä

Department of Biotechnology
Professor für Organische Chemie und Biochemie

Ulmenliet 20
21033 Hamburg

Room S2.33

T +49 40 428 75-6317
joerg.andrae_bt@haw-hamburg.de

Activities

Teaching

  • Organische Chemie
  • Biochemie
  • Biochemical Analytics
  • Mikrobiologisches und Molekularbiologisches Seminar
  • Research Projects, Bachelor- und Masterarbeiten

Focus areas/Expertise

  • Peptide des angeborenen Immunsystems als Leitstrukturen zur Entwicklung von antibiotischen, anti-entzündlichen und anti-Tumor Wirkstoffen
  • Abbaubare Antibiotika auf Peptidbasis (PharmCycle)
  • Bakterielle und eukaryotische Zellmembranmodelle

 

Aktuelle Drittmittel

bioSurf - Biotechnologische Herstellung von antimikrobiellen Peptiden und deren Verwendung als biozide Oberflächenbeschichtung (biocide surface)

C4T301 / BWFG

Offices held/Professional memberships

  • Departmentleiter Biotechnologie
  • Laborleitung Projektlabor
  • Departmentrat Biotechnologie
  • Forschungsgruppe PharmCycle
  • Forschungs- und Transferzentrum ALSTER (Applied Life Science Technologies and Environmental Research)
  • Participating Investigator Consortium for Functional Glycomics (CFG)

Professionelle Mitgliedschaften

  • Gesellschaft deutscher Chemiker (GdCh)
  • Gesellschaft für Biochemie und Molekularbiologie (GBM)
  • Hochschullehrerbund (Hlb)

Thesis (B.A./M.A.) and PhD supervision

Doktorarbeiten

Dominik Wilms (2012-2016)
Bedeutung von Oberflächenstrukturen für die selektive Aktivität von Antimikrobiellen Peptiden gegen Krebszellen.
In Kooperation mit der Universität zu Lübeck (Prof. Dr. Thomas Gutsmann)

Stephanie Gross (2011-2015)
Evaluation of antimicrobial peptides as anti-cancer agents against equine sarcoid and human prostate adenocarcionoma cells.
In Kooperation mit der Freien Universität Berlin (Prof. Dr. Susanne Hartmann).

Short bio

Chemiestudium in Bonn und Hamburg

Promotion am Bernhard-Nocht-Institut für Tropenmedizin, Hamburg

Habilitation und Privatdozentur für das Fach Biochemie an der Universität Hamburg

Wissenschaftlicher Mitarbeiter am Leibniz-Zentrum für Medizin und Biowissenschaften, Borstel

Postdoctoral Fellowship der Japan Society for the Promotion of Sciences (JSPS) in Takamatsu, Japan

Professur für Organische Chemie und Biochemie, HAW HAmburg

publications

Selected peer-reviewed papers

Bleibaum F, Sommer A, Veit M, Rabe B, Andrä J, Kunzelmann K, Nehls C, Correa W, Gutsmann T, Grötzinger J, Bhakdi S, Reiss K (2019) ADAM10 sheddase activation is controlled by cell membrane asymmetry. J Mol Cell Biol., 11:979-993

Andrä J, Beyer F, Cornelissen G, Einfeldt J, Heseding J, Kümmerer K, Oelkers K, Floeter C. PharmCycle: a holistic approach to reduce the contamination of the aquatic environment with antibiotics by developing sustainable antibiotics, improving the environmental risk assessment of antibiotics, and reducing the discharges of antibiotics in the wastewater outlet. Environ. Sci. Eur. 2018; 30:24 (https://rdcu.be/2LXp)

Veit M, Koyro KI, Ahrens B, Bleibaum F, Munz M, Rövekamp H, Andrä J, Schreiber R, Kunzelmann K, Sommer A, Bhakdi S, Reiss K. Anoctamin-6 regulates ADAM sheddase function. Biochim Biophys Acta Mol Cell Res. 2018; 1865:1598

Wilms D, Andrä J. Comparison of patient-derived high and low phosphatidylserine-exposing colorectal carcinoma cells in their Interaction with anti-cancer peptides. J. Pept. Sci. 2017; 23: 56

Sommer A, Kordowski F, Büch J, Maretzky T, Evers A, Andrä J, Düsterhöft S, Michalek M, Lorenzen I, Somasundaram P, Tholey A, Sönnichsen FD, Kunzelmann K, Heinbockel L, Nehls C, Gutsmann T, Grötzinger J, Bhakdi S, Reiss K. Phosphatidylserine exposure is required for ADAM17 sheddase function. Nat Commun. 2016; 7: 11523

Maletzki C, Klier U, Marinkovic S, Klar E, Andrä J, Linnebacher M. Host defense peptides for treatment of colorectal carcinoma - a comparative in vitro and in vivo analysis. Oncotarget. 2014; 5: 4467-4479

Gross S, Wilms D, Krause J, Brezesinski G, Andrä J. Design of NK-2-derived peptides with improved activity against equine sarcoid cells. J. Pept. Sci. 2013; 19: 619–628

Bankovic J*, Andrä J*, Todorovic N, Ana P-R, Ðor?e M, Jannike K, Ruždijic S, Tanic N, Pešic M. The elimination of P-glycoprotein over-expressing cancer cells by antimicrobial cationic peptide NK-2: the unique way of multi-drug resistance modulation. Exp. Cell Res. 2013; 319: 1013-1027. *equal contribution

Gross S, Andrä J. Anticancer peptide NK-2 targets cell surface sulphated glycans rather than sialic acids. Biol. Chem. 2012; 393: 817–827

Brandenburg K, Andrä J, Garidel P, Gutsmann T. Peptide-based treatment of sepsis. Appl. Microbiol. Biotechnol. 2011; 90: 799-808

Zweytick D, Deutsch G, Andrä J, Blondelle SE, Vollmer E, Jerala R, Lohner K. Studies on lactoferricin derived E. coli membrane active peptides reveal differences in the mechanism of N-acylated versus non-acylated peptides. J. Biol. Chem. 2011; 286: 21266-21276

Drechlser S, Andrä J. Online monitoring of metabolism and morphology of peptide-treated neuroblastoma cancer cells and keratinocytes. J. Bioenerget. Biomem. 2011; 43: 275-285

Andrä J, Goldmann T, Ernst CM, Peschel A, Gutsmann T. Multiple peptide resistance factor (MPRF)-mediated resistance of staphylococcus aureus against antimicrobial peptides coincides with a modulated peptide interaction with artificial membranes comprising lysyl-phosphatidylglycerol. J. Biol. Chem. 2011; 286: 18692-18700

Hammer M, Brauser A, Olak C, Brezesinski G, Goldmann T, Gutsmann T, Andrä J. Lipopolysaccharide interaction is decisive for the activity of the antimicrobial peptide NK-2 against Escherichia coli and Proteus mirabilis. Biochem. J. 2010; 427: 477-488

Brandenburg K, Garidel P, Fukuoka S, Howe J, Koch MH, Gutsmann T, Andrä J. Molecular basis for endotoxin neutralization by amphipathic peptides derived from the alpha-helical cationic core-region of NK-lysin. Biophys. Chem. 2010; 150: 80-87

Andrä J, Hammer MU, Grötzinger J, Jakovkin I, Lindner B, Vollmer E, Fedders H, Leippe M, Gutsmann T. Significance of the cyclic structure and of arginine residues for the antibacterial activity of arenicin-1 and its interaction with phospholipid and lipopolysaccharide model membranes. Biol. Chem. 2009; 390: 337-349

Schromm AB, Alexander C, Gutsmann T, Andrä J, Stamme C. Pathogens in Sepsis: Gram-negative bacterial PAMPs and PRRs. In: Cavaillon J-M, Adrie C, editors. Sepsis and non-infectious systemic inflammation. From biology to critical care. Weinheim: Wiley-VHC Verlag GmbH & Co, 2009:79-108

Andrä J, Jakovkin I, Grötzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Structure and mode of action of the antimicrobial peptide arenicin. Biochem. J. 2008; 410: 113-122

Andrä J, Böhling A, Gronewold TMA, Schlecht U, Perpeet M, Gutsmann T. Surface acoustic wave biosensor as a tool to study the interaction of antimicrobial peptides with phospholipid and lipopolysaccharide model membranes. Langmuir 2008; 24: 9148-9153

Japelj B, Zorko M, Majerle A, Pristovsek P, Sanchez Gomez S, Martinez de Tejada G, Moriyon I, Blondelle SE, Brandenburg K, Andrä J, Lohner K, Jerala R. Acyl group as the central element of the structural organization of antimicrobial lipopeptide. J. Am. Chem. Soc. 2007; 129: 1022-1023

Chen X, Howe J, Andrä J, Rössle M, Richter W, Silva APGd, Krensky AM, Clayberger C, Brandenburg K. Biophysical analysis of the mechanisms of interaction of granulysin-derived peptides with enterobacterial endotoxins. Biochim. Biophys. Acta 2007; 1768: 2421-2431

Andrä J, Monreal D, Martinez de Tejada G, Olak C, Brezesinski G, Sanchez Gomez S, Goldmann T, Bartels R, Brandenburg K, Moriyon I. Rationale for the design of shortened derivatives of the NK-lysin derived antimicrobial peptide NK-2 with improved activity against Gram-negative pathogens. J. Biol. Chem. 2007; 282: 14719-14728

Andrä J, Gutsmann T, Garidel P, Brandenburg K. Mechanisms of endotoxin neutralization by synthetic cationic compounds. J. Endotox. Res. 2006; 12: 261-277

Willumeit R, Kumpugdee M, Funari S, Lohner K, Pozo Navas B, Brandenburg K, Linser S, Andrä J. Structural rearrangement of model membranes by the peptide antibiotic NK–2. Biochim. Biophys. Acta 2005; 1669: 125-134

Schröder-Borm H, Bakalova R, Andrä J. The NK-lysin derived peptide NK-2 preferentially kills cancer cells with increased surface levels of negatively charged phosphatidylserine. FEBS Lett. 2005; 579: 6128-6134

Andrä J, Lohner K, Blondelle SE, Jerala R, Moriyon I, Koch MHJ, Garidel P, Brandenburg K. Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide. Biochem. J. 2005; 385: 135-143

Andrä J, Koch MHJ, Bartels R, Brandenburg K. Biophysical characterization of the endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-Lysin. Antimicrob. Agents Chemother. 2004; 48: 1593-1599

Andrä J, Berninghausen O, Leippe M. Membrane lipid composition protects Entamoeba histolytica from self-destruction by its pore-forming toxins. FEBS Lett. 2004; 564: 109-115

Schröder-Borm H, Willumeit R, Brandenburg K, Andrä J. Molecular basis for membrane selectivity of NK-2, a potent peptide antibiotic derived from NK-lysin. Biochim. Biophys. Acta 2003; 1612: 164-171

Andrä J, Halter R, Kock MA, Niemann H, Vogel CW, Paul D. Generation and characterization of transgenic mice expressing cobra venom factor. Mol. Immunol. 2002; 39: 357-365
 

Patents

Blondelle SE, Jerala R, Pristovsek P, Majerle A, Zorko M, Japelj B, Brandenburg K, Andrä J, Porro M, Moriyón I, León JL, Martinez de Tejada G, Zweytick D, Deutsch G, Lohner K, Antimicrobial peptides, Patent: WO 2008006125 (A1) 2008-01-17

Blondelle SE, Jerala R, Pristovsek P, Majerle A, Zorko M, Japelj B, Brandenburg K, Andrä J, Porro M, Moriyón I, León JL, Martinez de Tejada G, Zweytick D, Deutsch G, Lohner K (2006) Antimicrobial Peptides. in Austrian Patent Office, A 1165/2006  C07K, Austria

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