Search

Your search keyword '"Sewald N"' showing total 465 results
Start Over Author "Sewald N"
465 results on '"Sewald N"'

1. tubulin-cryptophycin complex

Author

Abel, A.C., primary, Muehlethaler, T., additional, Dessin, C., additional, Steinmetz, M.O., additional, Sewald, N., additional, and Prota, A.E., additional

Published
2024
Full Text
View/download PDF

5. Antiproliferative activity of a new xanthone derivative from leaves of Garcinia nobilis Engl.

Author

Fouotsa, Hugues, Dzoyem, Jean Paul, Lannang, Alain Meli, Stammler, Hans Georg, Mbazoa, Celine Djama, Luhmer, Michel, Nkengfack, Augustin Ephrem, Allémann, Éric, Delie, Florence, Meyer, Franck, Sewald, N., Fouotsa, Hugues, Dzoyem, Jean Paul, Lannang, Alain Meli, Stammler, Hans Georg, Mbazoa, Celine Djama, Luhmer, Michel, Nkengfack, Augustin Ephrem, Allémann, Éric, Delie, Florence, Meyer, Franck, and Sewald, N.

Abstract

A new xanthone, mboudiexanthone (1), together with five known compounds, euxanthone (2), isogarcinol (3), garcinol (4), betulinic acid (5) and zeorin (6) were isolated from the leaves of Garcinia nobilis Engl. The structures were determined by 1D and 2D NMR techniques and X-ray diffraction for 6. The in vitro antiproliferative properties of isolated compounds were evaluated against the human breast cancer cell line MCF-7. All compounds showed an antiproliferative activity with an IC50 value down to ∼11 µM for isogarcinol., SCOPUS: ar.j, info:eu-repo/semantics/published

Published
2021

6. Synthesis and biological evaluation of RGD–cryptophycin conjugates for targeted drug delivery

Author

Borbely A., Figueras E., Martins A., Esposito S., Auciello G., Monteagudo E., Di Marco A., Summa V., Cordella P., Perego R., Kemker I., Frese M., Gallinari P., Steinkuhler C., Sewald N., Borbely, A., Figueras, E., Martins, A., Esposito, S., Auciello, G., Monteagudo, E., Di Marco, A., Summa, V., Cordella, P., Perego, R., Kemker, I., Frese, M., Gallinari, P., Steinkuhler, C., and Sewald, N.

Subjects
Drug delivery, Antitumor agent, Small molecule–drug conjugates, RGD peptide
Abstract

Cryptophycins are potent tubulin polymerization inhibitors with picomolar antiproliferative potency in vitro and activity against multidrug-resistant (MDR) cancer cells. Because of neurotoxic side effects and limited efficacy in vivo, cryptophycin-52 failed as a clinical candidate in cancer treatment. However, this class of compounds has emerged as attractive payloads for tumor-targeting applications. In this study, cryptophycin was conjugated to the cyclopeptide c(RGDfK), targeting integrin αvβ3, across the protease-cleavable Val-Cit linker and two different self-immolative spacers. Plasma metabolic stability studies in vitro showed that our selected payload displays an improved stability compared to the parent compound, while the stability of the conjugates is strongly influenced by the self-immolative moiety. Cathepsin B cleavage assays revealed that modifications in the linker lead to different drug release profiles. Antiproliferative effects of Arg-Gly-Asp (RGD)–cryptophycin conjugates were evaluated on M21 and M21-L human melanoma cell lines. The low nanomolar in vitro activity of the novel conjugates was associated with inferior selectivity for cell lines with different integrin αvβ3 expression levels. To elucidate the drug delivery process, cryptophycin was replaced by an infrared dye and the obtained conjugates were studied by confocal microscopy.

Published
2019

24. Integrin 51: A new purification strategy based on immobilized peptides

Author

Wobbe, L., Zimmermann, D., Wißbrock, M., Urman, S., Sewald, K., Maleevi, M., Sewald, N., and Publica

Abstract

Novel efficient and robust affinity chromatography material: There are several strategies known for the purification of integrins by affinity chromatography, but the disadvantages of common strategies like insufficient selectivity or compelling conditions for the elution still require alternatives. A new strategy, based on the immobilized C-terminally modified peptide Ac-Gly-Ala-c-(CysSS-Arg-Arg-Glu-Thr-Ala-Trp-Ala-Cys SS)-Gly-Ala-O(CH2CH2O)2CH 2CH2-NH2 allows for the affinity purification of the integrin 51. While RGD peptides have been proven in the past to be inappropriate for selective purification of integrins by affinity chromatography, the new peptide can be efficiently used for selective enrichment of the integrin 51. It is a specific ligand of the target protein, but does not contain an RGD sequence. The application of well-characterized affinity chromatography material with a site-specifically immobilized peptide allows to obtain integrin 51 in a single chroma tography step without contamination by other integrins. This process combines the advantages of a selective and monospecific protein-ligand recognition with mild elution conditions and a low sensitivity of the immobilized ligand with respect to column regeneration.

Published
2005

Catalog

Books, media, physical & digital resources
See catalog results