In vitro display evolution of the PURE system-expressed TNFα-binding unnatural cyclic peptide containing an N-methyl-d-amino acid
| Autor: | Mizuki Yamamoto, Keita Tsukamoto, Yukio Takamori, Takashi Kawakami, Daisuke Horiuchi, Rina Iwamoto, Takehiro Ando, Takumi Yokoyama, Daisuke Fuji |
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| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Phenylalanine Biophysics Peptide Methylation Peptides Cyclic Biochemistry 03 medical and health sciences 0302 clinical medicine Peptide Library Humans mRNA display RNA Messenger Peptide library Molecular Biology chemistry.chemical_classification Tumor Necrosis Factor-alpha SELEX Aptamer Technique Cell Biology Cyclic peptide Amino acid 030104 developmental biology chemistry Genetic Code 030220 oncology & carcinogenesis Tumor necrosis factor alpha Systematic evolution of ligands by exponential enrichment Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 534:519-525 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2020.11.050 |
| Popis: | Tumor necrosis factor-alpha (TNFα) is a multifunctional cytokine associated with inflammation, immune responses, and autoimmune diseases including rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In the present study, we performed in vitro selection, systematic evolution of ligands by exponential enrichment (SELEX) against human TNFα from mRNA-displayed peptide library prepared with Escherichia coli-reconstituted cell-free transcription/translation system (PURE system) and cyclized by N-chloroacetyl-N-methyl- d -phenylalanine incorporated by genetic code expansion (sense suppression). We identified a novel TNFα-binding thioether-cyclized peptide that contains an N-methyl- d -phenylalanine. Since cyclic structure and presence of an N-methyl- d -amino acid can increase proteolytic stability, the TNFα binding peptide has potential to be used for therapeutic, research and diagnostic applications. |
| Databáze: | OpenAIRE |
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