Structure of a hydrophobic leucinostatin derivative determined by host lattice display.
Acta Crystallogr D Struct Biol
; 78(Pt 12): 1439-1450, 2022 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-36458615
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.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos Catiônicos Antimicrobianos
/
Aminoácidos
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Ano de publicação:
2022
Tipo de documento:
Article
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