Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion

Autor: Camilla Bertel Andersen, Jannik Nedergaard Pedersen, Jørn Døvling Kaspersen, Daniel E. Otzen, Jens Kvist Madsen, Kell K. Andersen, Jan Skov Pedersen

Publikováno v: Madsen, J K, Kaspersen, J D, Andersen, C B, Nedergaard Pedersen, J, Andersen, K K, Pedersen, J S & Otzen, D E 2017, ' Glycolipid Biosurfactants Activate, Dimerize, and Stabilize Thermomyces lanuginosus Lipase in a pH-Dependent Fashion ', Biochemistry, vol. 56, no. 32, pp. 4256-4268 . https://doi.org/10.1021/acs.biochem.7b00420

We present a study of the interactions between the lipase from Thermomyces lanuginosus (TlL) and the two microbially produced biosurfactants (BSs), rhamnolipid (RL) and sophorolipid (SL). Both RL and SL are glycolipids; however, RL is anionic, while

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https://doi.org/10.1021/acs.biochem.7b00420

Refolding of SDS-Unfolded Proteins by Nonionic Surfactants

Autor: Jørn Døvling Kaspersen, Jan Skov Pedersen, Daniel E. Otzen, Daniel Jhaf Madsen, Anne Sofie Søndergaard

Publikováno v: Kaspersen, J D, Søndergaard, A, Madsen, D J, Otzen, D E & Pedersen, J S 2017, ' Refolding of SDS-Unfolded Proteins by Nonionic Surfactants ', Biophysical Journal, vol. 112, no. 8, pp. 1609-1620 . https://doi.org/10.1016/j.bpj.2017.03.013

The strong and usually denaturing interaction between anionic surfactants (AS) and proteins/enzymes has both benefits and drawbacks: for example, it is put to good use in electrophoretic mass determinations but limits enzyme efficiency in detergent f

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https://pure.au.dk/ws/files/117313396/1_s2.0_S0006349517303326_main.pdf

How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro

Autor: Brian S. Vad, Yuichi Yoshimura, Cristine Betzer, Jørn Døvling Kaspersen, Frans A. A. Mulder, Camilla Bertel Andersen, Poul Henning Jensen, Gunna Christiansen, Nikolai Lorenzen, Daniel E. Otzen, Jan Skov Pedersen, Søren B. Nielsen

Publikováno v: Lorenzen, N, Nielsen, S B, Yoshimura, Y, Vad, B S, Andersen, C B, Betzer, C, Kaspersen, J D, Christiansen, G, Pedersen, J S, Jensen, P H, Mulder, F A A & Otzen, D E 2014, ' How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro ', Journal of Biological Chemistry, vol. 289, no. 31, pp. 21299-21310 . https://doi.org/10.1074/jbc.M114.554667

Oligomeric species of various proteins are linked to the pathogenesis of different neurodegenerative disorders. Consequently, there is intense focus on the discovery of novel inhibitors, e.g. small molecules and antibodies, to inhibit the formation a

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https://doi.org/10.1074/jbc.m114.554667

Generic Structures of Cytotoxic Liprotides:Nano-Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins

Autor: Sergei E. Permyakov, Ekaterina L. Nemashkalova, Jørn Døvling Kaspersen, Jan Skov Pedersen, Srinivasan Sakthivel, Eugene A. Permyakov, Jon Gade Hansted, Ludmilla A. Morozova-Roche, Daniel E. Otzen, Søren B. Nielsen, Jannik Nedergaard Pedersen, Cristiano L. P. Oliveira, Kristina Wilhelm

Publikováno v: Kaspersen, J D, Pedersen, J N, Hansted, J G, Nielsen, S B, Sakthivel, S, Wilhelm, K, Nemashkalova, E L, Permyakov, S E, Permyakov, E A, Pinto Oliveira, C L, Morozova-Roche, L A, Otzen, D & Pedersen, J S 2014, ' Generic Structures of Cytotoxic Liprotides : Nano-Sized Complexes with Oleic Acid Cores and Shells of Disordered Proteins ', ChemBioChem, vol. 10, no. 18, pp. 2693-2702 . https://doi.org/10.1002/cbic.201402407

The cytotoxic complex formed between α-lactalbumin and oleic acid (OA) has inspired many studies on protein-fatty acid complexes, but structural insight remains sparse. After having used small-angle X-ray scattering (SAXS) to obtain structural infor

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https://pure.au.dk/portal/da/publications/generic-structures-of-cytotoxic-liprotides(f8f41922-cdd0-411c-8a3a-f7d9d38ffd9a).html

The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation

Autor: Wojciech Paslawski, Tuomas P. J. Knowles, Alexander K. Buell, Maria Andreasen, Brian S. Vad, Søren B. Nielsen, Gunna Christiansen, Nikolai Lorenzen, Jørn Døvling Kaspersen, Zuzana Valnickova-Hansen, Daniel E. Otzen, Paolo Arosio, Jan J. Enghild, Jan Skov Pedersen, Christopher M. Dobson

Publikováno v: Lorenzen, N, Nielsen, S B, Buell, A K, Kaspersen, J D, Arosio, P, Vad, B S, Paslawski, W, Christiansen, G, Valnickova Hansen, Z, Andreasen, M, Enghild, J J, Pedersen, J S, Dobson, C M, Knowles, T P J & Otzen, D 2014, ' The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation ', Journal of the American Chemical Society, vol. 136, no. 10, pp. 3859-3868 . https://doi.org/10.1021/ja411577t

Studies of proteins' formation of amyloid fibrils have revealed that potentially cytotoxic oligomers frequently accumulate during fibril formation. An important question in the context of mechanistic studies of this process is whether or not oligomer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9edf33b60fabcb5b087bdc90dada8c7
https://pubmed.ncbi.nlm.nih.gov/24527756