Structure of a hydrophobic leucinostatin derivative determined by host lattice display

Kiss, Cedric; Gall, Flavio M.; Dreier, Birgit; Adams, Michael; Riedl, Rainer; Plückthun, Andreas; Mittl, Peer R. E.

doi:10.1107/S2059798322010762

Publication type:	Article in scientific journal
Type of review:	Peer review (publication)
Title:	Structure of a hydrophobic leucinostatin derivative determined by host lattice display
Authors:	Kiss, Cedric Gall, Flavio M. Dreier, Birgit Adams, Michael Riedl, Rainer Plückthun, Andreas Mittl, Peer R. E.
et. al:	No
DOI:	10.1107/S2059798322010762
Published in:	Acta Crystallographica. Section D: Structural Biology
Volume(Issue):	78
Issue:	12
Page(s):	1439
Pages to:	1450
Issue Date:	1-Dec-2022
Publisher / Ed. Institution:	Wiley
ISSN:	2059-7983
Language:	English
Subjects:	Crystal engineering; Host lattice display; Leucinostatin; Ribosome; X-ray diffraction; Antimicrobial cationic peptide; Amino acid
Subject (DDC):	572: Biochemistry
Abstract:	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
Fulltext version:	Published version
License (according to publishing contract):	Licence according to publishing contract
Departement:	Life Sciences and Facility Management
Organisational Unit:	Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:	Publikationen Life Sciences und Facility Management

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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.