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https://doi.org/10.21256/zhaw-26902| Publikationstyp: | Beitrag in wissenschaftlicher Zeitschrift |
| Art der Begutachtung: | Peer review (Publikation) |
| Titel: | Structure of a hydrophobic leucinostatin derivative determined by host lattice display |
| Autor/-in: | Kiss, Cedric Gall, Flavio M. Dreier, Birgit Adams, Michael Riedl, Rainer Plückthun, Andreas Mittl, Peer R. E. |
| et. al: | No |
| DOI: | 10.1107/S2059798322010762 10.21256/zhaw-26902 |
| Erschienen in: | Acta Crystallographica. Section D: Structural Biology |
| Band(Heft): | 78 |
| Heft: | 12 |
| Seite(n): | 1439 |
| Seiten bis: | 1450 |
| Erscheinungsdatum: | 1-Dez-2022 |
| Verlag / Hrsg. Institution: | Wiley |
| ISSN: | 2059-7983 |
| Sprache: | Englisch |
| Schlagwörter: | Crystal engineering; Host lattice display; Leucinostatin; Ribosome; X-ray diffraction; Antimicrobial cationic peptide; Amino acid |
| Fachgebiet (DDC): | 572: Biochemie |
| Zusammenfassung: | Peptides comprising many hydrophobic amino acids are almost insoluble under physiological buffer conditions, which complicates their structural analysis. To investigate the three-dimensional structure of the hydrophobic leucinostatin derivative ZHAWOC6027, the previously developed host lattice display technology was applied. Two designed ankyrin-repeat proteins (DARPins) recognizing a biotinylated ZHAWOC6027 derivative were selected from a diverse library by ribosome display under aqueous buffer conditions. ZHAWOC6027 was immobilized by means of the DARPin in the host lattice and the structure of the complex was determined by X-ray diffraction. ZHAWOC6027 adopts a distorted α-helical conformation. Comparison with the structures of related compounds that have been determined in organic solvents reveals elevated flexibility of the termini, which might be functionally important. |
| URI: | https://digitalcollection.zhaw.ch/handle/11475/26902 |
| Volltext Version: | Akzeptierte Version |
| Lizenz (gemäss Verlagsvertrag): | Lizenz gemäss Verlagsvertrag |
| Departement: | Life Sciences und Facility Management |
| Organisationseinheit: | Institut für Chemie und Biotechnologie (ICBT) |
| Enthalten in den Sammlungen: | Publikationen Life Sciences und Facility Management |
Dateien zu dieser Ressource:
| Datei | Beschreibung | Größe | Format | |
|---|---|---|---|---|
| 2022_Kiss-etal_Structure-of-hydrophobic-leucinostatin-derivative.pdf | Accepted Version | 3.82 MB | Adobe PDF |  Öffnen/Anzeigen |
Zur Langanzeige
Kiss, C., Gall, F. M., Dreier, B., Adams, M., Riedl, R., Plückthun, A., & Mittl, P. R. E. (2022). Structure of a hydrophobic leucinostatin derivative determined by host lattice display. Acta Crystallographica. Section D: Structural Biology, 78(12), 1439–1450. https://doi.org/10.1107/S2059798322010762
Kiss, C. et al. (2022) ‘Structure of a hydrophobic leucinostatin derivative determined by host lattice display’, Acta Crystallographica. Section D: Structural Biology, 78(12), pp. 1439–1450. Available at: https://doi.org/10.1107/S2059798322010762.
C. Kiss et al., “Structure of a hydrophobic leucinostatin derivative determined by host lattice display,” Acta Crystallographica. Section D: Structural Biology, vol. 78, no. 12, pp. 1439–1450, Dec. 2022, doi: 10.1107/S2059798322010762.
KISS, Cedric, Flavio M. GALL, Birgit DREIER, Michael ADAMS, Rainer RIEDL, Andreas PLÜCKTHUN und Peer R. E. MITTL, 2022. Structure of a hydrophobic leucinostatin derivative determined by host lattice display. Acta Crystallographica. Section D: Structural Biology. 1 Dezember 2022. Bd. 78, Nr. 12, S. 1439–1450. DOI 10.1107/S2059798322010762
Kiss, Cedric, Flavio M. Gall, Birgit Dreier, Michael Adams, Rainer Riedl, Andreas Plückthun, and Peer R. E. Mittl. 2022. “Structure of a Hydrophobic Leucinostatin Derivative Determined by Host Lattice Display.” Acta Crystallographica. Section D: Structural Biology 78 (12): 1439–50. https://doi.org/10.1107/S2059798322010762.
Kiss, Cedric, et al. “Structure of a Hydrophobic Leucinostatin Derivative Determined by Host Lattice Display.” Acta Crystallographica. Section D: Structural Biology, vol. 78, no. 12, Dec. 2022, pp. 1439–50, https://doi.org/10.1107/S2059798322010762.
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