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  • 1.
    Belfrage, Anna Karin
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Abdurakhmanov, Eldar
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry.
    Åkerblom, Eva
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Brandt, Peter
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Alogheli, Hiba
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Neyts, Johan
    Rega Institute, Department of Microbiology and Immunology, University of Leuven, B-3000 Leuven, Belgium.
    Danielson, U. Helena
    Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC.
    Johansson, Anja
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Pan-NS3 protease inhibitors of hepatitis C virus based on an R3-elongated pyrazinone scaffold2018In: European Journal of Medicinal Chemistry, ISSN 0223-5234, E-ISSN 1768-3254, Vol. 148, p. 453-464Article in journal (Refereed)
    Abstract [en]

    Herein, we present the design and synthesis of 2(1H)-pyrazinone based HCV NS3 protease inhibitors and show that elongated R-3 urea substituents were associated with increased inhibitory potencies over several NS3 protein variants. The inhibitors are believed to rely on beta-sheet mimicking hydrogen bonds which are similar over different genotypes and current drug resistant variants and correspond to the beta-sheet interactions of the natural peptide substrate. Inhibitor 36, for example, with a urea substituent including a cyclic imide showed balanced nanomolar inhibitory potencies against genotype la, both wild-type (K-i=30 nM) and R155K (K-i=2 nM), and genotype 3a (K-i=5 nM).

  • 2.
    Chinthakindi, Praveen K.
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Arvidsson, Per I.
    Univ KwaZulu Natal, Catalysis & Peptide Res Unit, Durban, South Africa;Karolinska Inst, Sci Life Lab, Drug Discovery & Dev Platform, Stockholm, Sweden;Karolinska Inst, Div Translat Med & Chem Biol, Dept Med Biochem & Biophys, Stockholm, Sweden.
    Sulfonyl Fluorides (SFs): More Than Click Reagents?2018In: European Journal of Organic Chemistry, ISSN 1434-193X, E-ISSN 1099-0690, no 27-28, p. 3648-3666Article, review/survey (Refereed)
    Abstract [en]

    Sulfonyl fluoride (SF) containing substances are currently attracting enormous attention among practitioners of both chemical biology and synthetic organic chemistry. The groups of Jones and Liskamp have demonstrated the potential of sulfonyl fluorides as selective covalent inhibitors in studies related to drug discovery and chemical biology, respectively, in the last few years. The Sharpless group has extended the repertoire of click-reactions to those involving sulfonyl fluorides, that is, sulfur-fluoride exchange (SuFEx), a development that quickly triggered the interest in this functional group in the community of synthetic organic chemists. In this microreview, we aim to give an account of the synthetic chemistry surrounding sulfonyl fluoride containing substances from a historical perspective to present day developments.

  • 3.
    Chinthakindi, Praveen K.
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Benediktsdottir, Andrea
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Ibrahim, Ayah
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Wared, Atta
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Aurell, Carl-Johan
    AstraZeneca, Large Scale Chem, Early Chem Dev, Pharmaceut Sci,IMED Biotech Unit, S-43183 Gothenburg, Sweden.
    Pettersen, Anna
    AstraZeneca, Early Prod Dev, Pharmaceut Sci, IMED Biotech Unit, S-43183 Gothenburg, Sweden.
    Zamaratski, Edouard
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Arvidsson, Per I.
    Karolinska Inst, Sci Life Lab, Drug Discovery & Dev Platform, S-17177 Stockholm, Sweden;Karolinska Inst, Dept Med Biochem & Biophys, Div Translat Med & Chem Biol, S-17177 Stockholm, Sweden;Univ KwaZulu Natal, Catalysis & Peptide Res Unit, ZA-4000 Durban, South Africa.
    Chen, Yantao
    AstraZeneca, Med Chem, Cardiovasc Renal & Metab, IMED Biotech Unit, S-43183 Gothenburg, Sweden.
    Sandström, Anja
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Synthesis of Sulfonimidamide-Based Amino Acid Building Blocks with Orthogonal Protecting Groups2019In: European Journal of Organic Chemistry, ISSN 1434-193X, E-ISSN 1099-0690, no 5, p. 1045-1057Article in journal (Refereed)
    Abstract [en]

    Herein, we report the synthesis of novel sulfonimidamides (SIAs) based on amino acid building blocks using a one-pot method from tert-butyldiphenylsilyl-protected (TBDPS) sulfonamides, as well as exploration of orthogonal deprotection strategies. Among the several protecting groups investigated, TBDPS showed higher conversion, allowed UV detection and simple diastereomeric separation; in particular in combination with amino acid tert-butyl esters. Moreover, we applied the present method to synthesize cyclic five-membered acyl sulfonimidamides in two steps. The described synthesis of SIA-based amino acid building blocks in combination with the orthogonal protection groups provide access to unnatural amino acid building blocks useful for further incorporation into larger molecules, such as peptide-based transition-state analogues and peptidomimetics. The chirality of the SIA group, as well as its additional point of diversity provided by the extra NH group, creates opportunities for the development of unique compound libraries that explore new chemical space, which is of considerable importance for the pharmaceutical and agrochemical industry.

  • 4.
    Rodrigues, Leticia
    et al.
    Ludwig Maximilians Univ Munchen, Dept Pharm Pharmaceut Technol & Biopharm, Butenandtstr 5-13, DE-81377 Munich, Germany.
    Schneider, Fabian
    Tech Univ Munich, Walter Schottky Inst, Phys Dept, Coulombwall 4a, DE-85748 Garching, Germany;Tech Univ Munich, Walter Schottky Inst, Inst Adv Study, Coulombwall 4a, DE-85748 Garching, Germany.
    Zhang, Xiaohan
    Tech Univ Munich, Soft Matter Phys Grp, Phys Dept, James Franck Str 1, DE-85748 Garching, Germany.
    Larsson, Elin
    Umea Univ, Dept Integrat Med Biol, Johan Bures Vag 12, SE-90187 Umea, Sweden.
    Moodie, Lindon W. K.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery. Umea Univ, Dept Chem, Linnaeus Vag 1, SE-90736 Umea, Sweden.
    Dietz, Hendrik
    Tech Univ Munich, Walter Schottky Inst, Phys Dept, Coulombwall 4a, DE-85748 Garching, Germany;Tech Univ Munich, Walter Schottky Inst, Inst Adv Study, Coulombwall 4a, DE-85748 Garching, Germany.
    Papadakis, Christine M.
    Tech Univ Munich, Soft Matter Phys Grp, Phys Dept, James Franck Str 1, DE-85748 Garching, Germany.
    Winter, Gerhard
    Ludwig Maximilians Univ Munchen, Dept Pharm Pharmaceut Technol & Biopharm, Butenandtstr 5-13, DE-81377 Munich, Germany.
    Lundmark, Richard
    Umea Univ, Dept Integrat Med Biol, Johan Bures Vag 12, SE-90187 Umea, Sweden.
    Hubert, Madlen
    Umea Univ, Dept Integrat Med Biol, Johan Bures Vag 12, SE-90187 Umea, Sweden.
    Cellular uptake of self-assembled phytantriol-based hexosomes is independent of major endocytic machineries2019In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 553, p. 820-833Article in journal (Refereed)
    Abstract [en]

    Despite increasing interests in non-lamellar liquid crystalline dispersions, such as hexosomes, for drug delivery, little is known about their interactions with cells and mechanism of cell entry. Here we examine the cellular uptake of hexosomes based on phytantriol and mannide monooleate by HeLa cells using live cell microscopy in comparison to conventional liposomes. To investigate the importance of specific endocytosis pathways upon particle internalization, we silenced regulatory proteins of major endocytosis pathways using short interfering RNA. While endocytosis plays a significant role in liposome internalization, hexosomes are not taken up via endocytosis but through a mechanism that is dependent on cell membrane tension. Biophysical studies using biomembrane models highlighted that hexosomes have a high affinity for membranes and an ability to disrupt lipid layers. Our data suggest that direct biomechanical interactions of hexosomes with membrane lipids play a crucial role and that the unique morphology of hexosomes is vital for their membrane activity. Based on these results, we propose a mechanism, where hexosomes destabilize the bilayer, allowing them to "phase through" the membrane. Understanding parameters that influence the uptake of hexosomes is critical to establish them as carrier systems that can potentially deliver therapeutics efficiently to intracellular sites of action.

  • 5.
    Skogh, Anna
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Lesniak, Anna
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Sköld, Christian
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Karlgren, Maria
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmacy.
    Gaugaz, Fabienne Z.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmacy. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Svensson, Richard
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmacy. Uppsala University, Science for Life Laboratory, SciLifeLab.
    Diwakarla, Shanti
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Jonsson, Anna
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Fransson, Rebecca
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry.
    Nyberg, Fred
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Hallberg, Mathias
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
    Johansson, Anja
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    An imidazole based H-Phe-Phe-NH2 peptidomimetic with anti-allodynic effect in spared nerve injury mice2018In: Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, E-ISSN 1090-2120, Vol. 28, no 14, p. 2446-2450Article in journal (Refereed)
    Abstract [en]

    The dipeptide amide H-Phe-Phe-NH2 (1) that previously was identified as a ligand for the substance P 1-7 (SP1-7) binding site exerts intriguing results in animal models of neuropathic pain after central but not after peripheral administration. The dipeptide 1 is derived from stepwise modifications of the anti-nociceptive heptapeptide SP1-7 and the tetrapeptide endomorphin-2 that is also binding to the SP1-7 site. We herein report a strong anti-allodynic effect of a new H-Phe-Phe-NH2 peptidomimetic (4) comprising an imidazole ring as a bioisosteric element, in the spare nerve injury (SNI) mice model after peripheral administration. Peptidomimetic 4 was stable in plasma, displayed a fair membrane permeability and a favorable neurotoxic profile. Moreover, the effective dose (ED50) of 4 was superior as compared to gabapentin and morphine that are used in clinic.

  • 6.
    Söderström, Marcus
    et al.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Zamaratski, Edouard
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Drug Design and Discovery.
    Odell, Luke R.
    Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Preparative Medicinal Chemistry.
    Thiomethylation, Nitro Reduction and Tandem Reduction/SMe Insertion of Nitrogen Heterocycles Using BF3⦁SMe2In: European Journal of Organic Chemistry, ISSN 1434-193X, E-ISSN 1099-0690Article in journal (Refereed)
    Abstract [en]

    Herein, a general, solvent-free and straightforward thiomethylation of electron deficient heterocycles using BF3⦁SMe2 as a dual thiomethyl source and Lewis acidic activator is presented. A range of heterocycles including pyrimidine, pyrazine, pyridazine, thiazole and purine derivatives were successfully substituted using this method. An unexpected reductive property of BF3⦁SMe2

    towards nitropyridines was also discovered including an intriguing tandem reduction/SMe insertion process in certain substrates. Notable features of the present work include its convenience and use of a non-malodorous reagent while the discovery of novel chemical transformations using BF3⦁SMe2 provides fundamental new insights into the reactivity of this commonly employed reagent.

1 - 6 of 6
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