PubMed
Reposit HAW-Hamburg
Selected peer-reviewed papers
Schromm AB. Paulowski L, Kaconis Y, Kopp F, Koistinen M, Donoghue A, Keese S, Nehls C, Wernecke J, Garidel P, Sevcsik E, Lohner K, Sanchez-Gomez S, Martinez-de-Tejada G, Brandenburg K, Brameshuber M, Schütz GJ, Andrä J, Gutsmann T. (2021) Cathelicidin and PMB neutralize endotoxins by multifactorial mechanisms including LPS interaction and targeting of host cell membranes. Proceedings of the National Academy of Sciences of the United States of America 118: (DOI: 10.1073/pnas.2101721118)
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
