de Jalón, EG., Kleinmanns, K., Fosse, V., Davidson, B., Bjørge, L., Haug, B.E.*, McCormack, E.*
Comparison of five near-infrared fluorescent folate conjugates in an ovarian cancer model.
Molecular Imaging and Biology, 2021.
https://doi.org/10.1007/s11307-021-01685-y
Espeland, L.O., Georgiou, C., Klein, R., Bhukya, H., Haug, B.E., Underhaug, J., Mainkar, P.S., Brenk, R.
An experimental toolbox for structure-based hit discovery for P. aeruginosa FabF, a promising target for antibiotics.
ChemMedChem, 2021, 16(17), 2715-2726.
https://doi.org/10.1002/cmdc.202100302
de Jalón, E.G., de Garibay, G.R., Haug, B.E.*, McCormack, E*.
CytoCy5S™, a compound of many structures. in vitro and in vivo evaluation of four near-infrared fluorescent substrates of nitroreductase (NTR).
Dyes and Pigments, 2021, 196, 109553.
https://doi.org/10.1016/j.dyepig.2021.109553
de Garibay, G.R., de Jalón, E.G., Stigen, E., Lund, K.B., Popa, M., Davidson, B., Safont, M.M, Rygh, C.B., Espedal, H., Barrett, T.M., Haug, B.E., McCormack, E.
Repurposing 18F-FMISO as a PET tracer for translational imaging of nitroreductase-based gene directed enzyme prodrug therapy.
Theranostics, 2021, 11(12), 6044-6057.
https://doi:10.7150/thno.55092
Guttormsen, Y., Fairhurst, M. E., Pandey, S. K, Isaksson, J., Haug, B. E.*, Bayer, A.*
Total synthesis of phorbazole B.
Molecules, 2020, 25 (20), 4848.
https://doi.org/10.3390/molecules25204848
Ndukwe, I. E., Lam, Y.-H., Pandey,S. K., Haug, B. E., Bayer, A., Sherer, E. C., Blinov, K. A., Williamson, R. T., Isaksson, J., Reibarkh, M., Liu, Y., Martin, G. E.
Unequivocal Structure Confirmation of a Breitfussin Analog by Anisotropic NMR Measurements.
Chemical Science, 2020, 11, 12081-12088.
https://doi.org/10.1039/D0SC03664A
Hansen, K. O.*, Andersen, J. H., Bayer, A., Pandey, S. K., Lorentzen, M., Jorgensen, K. B., Sydnes, M. O., Guttormsen, Y., Baumann, M., Koch, U., Klebl, B., Eickhoff, J., Haug, B. E.*, Isaksson, J., Hansen, E. H.
Kinase Chemodiversity from the Arctic: The Breitfussins.
Journal of Medicinal Chemistry, 2019, 62 (22), 10167-10181.
https://doi.org/10.1021/acs.jmedchem.9b01006
Goris, M., Magin, R. S., Foyn, H., Myklebust, L. M., Drazic, A., Bhambra, P., Varland, S., Støve, S. I., Baumann, M., Haug, B. E., Marmorstein, R., Arnesen, T.
Structure, substrate specificity and selective inhibition of the actin N-terminal acetyltransferase Naa80.
Proceedings of the National Academy of Sciences (USA), 2018, 115 (17), 4405-4410.
https://doi.org/10.1073/pnas.1719251115
Fairhurst, M. E., Zeeshan, M., Haug, B.E.*, Bayer, A.*
Aldol condensations on a 3-alkylidene-2,5-diketopiperazine – synthesis of two marine natural products.
Synlett, 2018, 29 (10), 1303-1306.
https://doi.org/10.1055/s-0036-1591755
Nestvold, J., Wang, M.-Y., Camilio, K. A., Tjelle, T. E., Lindberg, A., Haug, B. E., Kvalheim, G., Sveinbjørnsson, B., Rekdal, Ø.
Oncolytic peptide LTX-315 induces an immune-mediated abscopal effect in a rat sarcoma model.
OncoImmunology, 2017, 6 (8), e1338236.
https://doi.org/10.1080/2162402X.2017.1338236
Baumann, M., Nome, L. M., Zachariassen, Z. G., Karlshøj, S., Fossen, T., Rosenkilde, M. M., Våbenø, J.*, Haug, B. E.*
Synthesis of a novel Tripeptidomimetic scaffold and biological evaluation for CXC chemokine receptor 4 (CXCR4) antagonism.
Tetrahedron, 2017, 73 (27), 3866-3877.
https://doi.org/10.1016/j.tet.2017.05.057
Sveinbjørnsson, B., Camilio, K. A., Haug, B. E., Rekdal, Ø.
LTX-315: A first in class oncolytic peptide that reprograms the tumor microenvironment.
Future Medicinal Chemistry, 2017, 9 (12), 1339-1344.
https://doi.org/10.4155/fmc-2017-0088
Baumann, M., Hussain, M. M., Henne, N., Garrote, D. M., Karlshøj, S., Fossen, T., Rosenkilde, M. M., Våbenø, J.*, Haug, B. E.*
Influence of chain length on the activity of tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4).
Bioorganic & Medicinal Chemistry, 2017, 25 (2), 646-657.
https://doi.org/10.1016/j.bmc.2016.11.036
Støve, S. I., Magin, R. S., Foyn, H., Haug, B. E., Marmorstein, R., Arnesen, T.
Crystal structure of the Golgi-associated human N-alpha acetyltransferase 60 (Naa60/NatF) reveals the molecular determinants for substrate-specific acetylation.
Structure, 2016, 24 (7), 1044-1056.
https://doi.org/10.1016/j.str.2016.04.020
Haug, B. E.*, Camilio, K. A., Eliassen, L. T., Stensen, W., Svendsen, J. S., Berg, K., Mortensen, B., Serin, G., Mirjolet, J.-F., Bichat, F., Rekdal, Ø.*
Discovery of a 9-mer cationic peptide (LTX-315) as a potential first in class oncolytic peptide.
Journal of Medicinal Chemistry, 2016, 59 (7), 2918-2927.
https://doi.org/10.1021/acs.jmedchem.5b02025
Aubi, O., Flydal, M. I., Zheng, H., Skjærven, L., Rekand, I., Leiros, H.-K. S., Haug, B. E., Cianciotto, N. P., Martinez, A., Underhaug, J.
Discovery of a specific inhibitor of pyomelanin synthesis in Legionella pneumophila.
Journal of Medicinal Chemistry, 2015, 58 (21), 8402-8412.
https://doi.org/10.1021/acs.jmedchem.5b01589
Zachariassen, Z. G., Karlshøj, S., Haug, B. E., Rosenkilde, M. M., Våbenø, J. Probing the molecular interactions between CXC chemokine receptor 4 (CXCR4) and an arginine-based tripeptidomimetic antagonist (KRH-1636).
J. Med. Chem., 2015, 58 (20), 8141-8153.
Våbenø, J., Haug, B. E., Rosenkilde, M. M., Progress toward rationally designed small-molecule peptide and peptidomimetic CXCR4 antagonists.
Future Med. Chem., 2015, 7(10), 1261-1283.
Liu, L., Budnjo, A., Jokela, J., Haug, B. E., Fewer, D., Wahlsten, M., Rouhiainen, L., Permi, P., Fossen, T., Sivonen, K. Pseudoaeruginosins, nonribosomal peptides in Nodularia spumigena.
ACS Chem. Biol., 2015, 10 (3), 725-733.
Pandey, S. K., Guttormsen, Y., Haug, B. E., Hedberg, C., Bayer, A. A concise total synthesis of breitfussin A and B.
Org. Lett., 2015, 17 (1), 122-125.
Budnjo, A., Narawane, S., Grauffel, C., Schillinger, A.-S., Fossen, T., Reuter, N.*, Haug, B. E.* Reversible ketomethylene-based inhibitors of human neutrophil proteinase 3.
J. Med. Chem., 2014, 57, 9396-9408.
Zachariassen, Z. G., Thiele, S., Berg, E. A., Rasmussen, P., Fossen, T., Rosenkilde, M. M., Våbenø, J.*, Haug, B. E.* Design, synthesis, and biological evaluation of scaffold-based tripeptidomimetic antagonists for CXC chemokine receptor 4 (CXCR4).
Bioorg. Med. Chem., 2014, 22, 4759-4769.
Narawane, S., Budnjo, A., Grauffel, C., Haug, B. E.*, Reuter, N.* In silico design, synthesis, and assays of specific substrates for proteinase 3: Influence of fluorogenic and charged groups.
J. Med. Chem., 2014, 57 (3), 1111–1115.
Harmsen, R. A. G., Sivertsen, A., Michetti, D., Brandsdal, B. O., Sydnes, L. K., Haug, B. E.* Synthesis and docking of novel piperidine renin inhibitors.
Monatsh. Chem., 2013, 144(4), 479-494.
McCormack, E., Silden, E., West, R. M., Pavlin, T., Micklem, D. R., Lorens, J., Haug, B. E., Cooper, M. E., Gjertsen, B. T. Nitroreductase, a near infrared reporter platform for in vivo time-domain optical imaging of metastatic cancer.
Cancer Res., 2013, 73(4), 1276-1286.
Steinkopf, S., Hanekam, L., Schaathun, M., Budnjo, A., Haug, B. E., Nerdal, W. Interaction of local anesthetic articaine enantiomers with brain lipids: A Langmuir monolayer study.
Eur. J. Pharm. Sci. 2012, 47(2), 394-401.
Farooq, T., Sydnes, L. K.*, Törnroos, K. W., Haug, B. E.* Debenzylation of functionalized N-benzyl 4- and 5-substituted 1,2,3-triazoles.
Synthesis, 2012, 44, 2070-2078.
Farooq, T., Haug, B. E.*, Sydnes, L. K.*, Törnroos, K. W. 1,3-Dipolar cycloaddition of benzyl azide with two highly functionalized alkynes.
Monatsh. Chem. 2012, 143(3), 505-512.
Rekdal, Ø., Haug, B. E., Kalaaji, M., Hunter, H. N., Lindin, I., Israelsson, I., Solstad, T., Yang, N., Brandl, M., Mantzilas, D., Jing, W., Vogel, H. The relative spatial positions of tryptophan and cationic residues in helical membrane-active peptides determines their cytotoxicity.
J. Biol. Chem., 2012, 287(1), 233-244.
Harmsen, R. A. G., Sydnes, L. K., Törnroos, K. W., Haug, B. E.*. Synthesis of trans-4-triazolyl-substituted 3-hydroxypiperidines.
Synthesis, 2011, 5, 749-754.
Skjevik, Å. A., Haug, B. E., Lygre, H., Teigen, K. Intramolecular hydrogen bonding in articaine can be related to superior bone tissue penetration. A molecular dynamics study.
Biophys. Chem., 2011, 154(1), 18-25.
Haug, B. E.*, Kalaaji, M., Rekdal, Ø., Stensen, W., Svendsen, J.S. Synthetic antimicrobial peptidomimetics with therapeutic potential.
J. Med. Chem. 2008, 51(14), 4306-4314.
Svenson, J., Brandsdal, B. O., Stensen, W., Haug, B. E., Svendsen, J. S. Antibacterial peptides with stability towards tryptic degradation.
Biochemistry. 2008, 47(12), 3777-3788.
Haug, B. E.*, Stensen, W., Svendsen, J. S. Application of the Suzuki-Miyaura cross-coupling to increase antimicrobial potency generates promising novel antibacterials.
Bioorg. Med. Chem. Lett. 2007, 17(8), 2361-2364.
Haug, B. E., Strøm, M. B., Svendsen, J. S. The medicinal chemistry of short lactoferricin-based antibacterial peptides.
Curr. Med. Chem. 2007, 14(1), 1-18.
Haug, B. E., Brewer, M., Rich, D. H. Facile degradative lactonization of Gln-Arg and Gln-Phe hydroxyethylene dipeptide derivatives.
J. Peptide. Res., 2005, 65(1): 77-83.
Haug, B. E., Rich, D. H. Synthesis of a Gln-Phe hydroxyethylene dipeptide isostere.
Org. Lett., 2004, 6(25): 4783-4786.
Haug, B. E., Stensen, W., Stiberg, T., Svendsen, J. S. Bulky non-proteinogenic amino acids permit the design of very small and effective cationic antibacterial peptides.
J. Med. Chem. 2004, 47(17): 4159-4162.
Eliassen, L. T., Haug, B. E., Berge, G., Rekdal, Ø. Enhanced antitumour activity of 15-residue bovine lactoferricin derivatives containing bulky aromatic amino acids and lipophilic N-terminal modifications.
J. Peptide Sci, 2003, 9(8): 510-517.
Strøm, M. B., Haug, B. E., Skar, M. L., Stensen, W., Stiberg, T., Svendsen, J. S. The pharmacophore of short cationic antibacterial peptides.
J. Med. Chem. 2003, 46(9): 1567-1570.
Haug, B. E., Andersen, J., Rekdal, Ø., Svendsen, J. S. Synthesis of a 2-arylsulfonylated tryptophan: The antibacterial activity of bovine lactoferricin peptides containing Trp(2-Pmc).
J. Peptide Sci. 2002, 8 (7): 307-313.
Lejon, T., Svendsen, J. S., Haug, B. E. Simple parameterisation of non-natural amino acids for QSAR of antibacterial peptides.
J. Peptide Sci. 2002, 8 (7): 302-306.
Strøm, M. B, Haug, B. E., Rekdal, Ø., Skar, M. L., Stensen, W., Svendsen, J. S. Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity.
Biochem. Cell. Biol. 2002, 80(1): 65-74.
Haug, B. E., Skar, M. L., Svendsen, J. S. Bulky aromatic amino acids increase the antibacterial activity of bovine lactoferricin peptides.
J. Peptide Sci. 2001, 7(8): 425-432.
Haug, B. E., Svendsen, J. S. The role of tryptophan in the antibacterial activity of a 15-residue bovine lactoferricin peptide.
J. Peptide Sci. 2001, 7(4): 190-196.