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In vitro display evolution of IL-6R-binding unnatural peptides ribosomally initiated and cyclized with m-(chloromethyl)benzoic acid.
- Source :
-
Biochemical & Biophysical Research Communications . Jan2021, Vol. 535, p47-53. 7p. - Publication Year :
- 2021
-
Abstract
- The interaction of the multifunctional cytokine interleukin (IL)-6 and its receptor (IL-6R) is involved in various diseases, including not only autoimmune diseases such as rheumatoid arthritis but also cancer and cytokine storms in coronavirus disease 2019 (COVID-19). In this study, systematic evolution of ligands by exponential enrichment (SELEX) against human IL-6R from mRNA-displayed unnatural peptide library ribosomally initiated and cyclized with m -(chloromethyl)benzoic acid (mClPh) incorporated by genetic code expansion (sense suppression) was performed using the PURE (Protein synthesis Using Recombinant Elements) system. A novel 13-mer unnatural mClPh-cyclized peptide that binds to the extracellular domain of IL-6R was discovered from an extremely diverse random peptide library. In vitro affinity maturation of IL-6R-binding unnatural mClPh-cyclized peptide from focused libraries was performed, identifying two IL-6R-binding unnatural mClPh-cyclized peptides by next-generation sequencing. Because cyclization can increase the protease resistance of peptides, novel IL-6R-binding mClPh-cyclized peptides discovered in this study have the potential to be used for a variety of research, therapeutic, and diagnostic applications involving IL-6/IL-6R signaling. • m-(Chloromethyl)benzoic acid was ribosomally incorporated by genetic code expansion. • mRNA-displayed peptide library was cyclized with m-(chloromethyl)benzoic acid. • Systematic Evolution of Ligands by EXponential enrichment (SELEX) was performed. • A novel IL-6R-binding unnatural thioether-cyclized peptide was discovered. • In vitro affinity maturation of IL-6R-binding unnatural cyclic peptide was performed. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0006291X
- Volume :
- 535
- Database :
- Academic Search Index
- Journal :
- Biochemical & Biophysical Research Communications
- Publication Type :
- Academic Journal
- Accession number :
- 147945202
- Full Text :
- https://doi.org/10.1016/j.bbrc.2020.11.123