Structure of a hydrophobic leucinostatin derivative determined by host lattice display
| Autor: | Kiss, Cedric, Gall, Flavio M, Dreier, Birgit, Adams, Michael, Riedl, Rainer, Plückthun, Andreas, Mittl, Peer R E |
|---|---|
| Přispěvatelé: | University of Zurich |
| Rok vydání: | 2022 |
| Předmět: |
Antimicrobial cationic peptide
572: Biochemie Crystal engineering Leucinostatin 610 Medicine & health Ribosome X-ray diffraction Amino acid 1315 Structural Biology Structural Biology 10019 Department of Biochemistry 570 Life sciences biology Amino Acids Ribosomes Host lattice display Antimicrobial Cationic Peptides |
| Zdroj: | Acta Crystallographica Section D Structural Biology. 78:1439-1450 |
| ISSN: | 2059-7983 |
| DOI: | 10.1107/s2059798322010762 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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