Human interleukin-23 receptor antagonists derived from an albumin-binding domain scaffold inhibit IL-23-dependent ex vivo expansion of IL-17-producing T-cells

ABSTRACT Engineered combinatorial libraries derived from small protein scaffolds represent a powerful tool for generating novel binders with high affinity, required specificity and designed inhibitory function. This work was aimed to generate a collection of recombinant binders of human interleukin‐...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2014-06, Vol.82 (6), p.975-989
Hauptverfasser:	Kuchař, Milan, Vaňková, Lucie, Petroková, Hana, Černý, Jiří, Osička, Radim, Pelák, Ondřej, Šípová, Hana, Schneider, Bohdan, Homola, Jiří, Šebo, Peter, Kalina, Tomáš, Malý, Petr
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anti-Inflammatory Agents - chemistry Anti-Inflammatory Agents - pharmacology Bacterial Proteins - chemistry Binding, Competitive combinatorial library cytokine Drug Evaluation, Preclinical engineered binding protein Humans Immunologic Factors - chemistry Immunologic Factors - pharmacology Interleukin-23 - chemistry Interleukin-23 - physiology Jurkat Cells K562 Cells Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - pharmacology Protein Binding protein scaffold psoriasis Receptors, Interleukin - antagonists & inhibitors Receptors, Interleukin - physiology ribosome display Sequence Homology, Amino Acid Streptococcus Th17 Cells - drug effects Th17 Cells - metabolism
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