| Title | De novo design of helical peptides to inhibit tumor necrosis factor-alpha by disrupting its trimer formation |
| Authors | Shen, Qi Zhang, Changsheng Liu, Hongbo Liu, Yuting Cao, Junyue Zhang, Xiaolin Liang, Yuan Zhao, Meiping Lai, Luhua |
| Affiliation | Peking Univ, Ctr Quantitat Biol, Beijing 100871, Peoples R China. Peking Univ, State Key Lab Struct Chem Unstable & Stable Speci, BNLMS, Beijing 100871, Peoples R China. Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China. Peking Univ, Coll Chem & Mol Engn, BNLMS, Beijing 100871, Peoples R China. Peking Univ, Sch Life Sci, Beijing 100871, Peoples R China. Peking Univ, Ctr Quantitat Biol, Beijing 100871, Peoples R China. Lai, LH (reprint author), Peking Univ, State Key Lab Struct Chem Unstable & Stable Speci, BNLMS, Beijing 100871, Peoples R China. Lai, LH (reprint author), Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China. Lai, LH (reprint author), Peking Univ, Coll Chem & Mol Engn, BNLMS, Beijing 100871, Peoples R China. |
| Keywords | SMALL-MOLECULE INHIBITORS TNF-ALPHA FACTOR ANTAGONISTS BINDING OLIGOMERIZATION SUPERFAMILY RECEPTORS DISCOVERY DOMAIN |
| Issue Date | 2016 |
| Publisher | MEDCHEMCOMM |
| Citation | MEDCHEMCOMM.2016,7,(4),725-729. |
| Abstract | A computational strategy was used to design helical peptides that can bind to tumor necrosis factor-alpha (TNF alpha) dimers to prevent active trimer formation. Three designed peptides showed TNF alpha inhibition at the cellular level. Chemical crosslinking and mass spectrometry studies verified that these peptides function by breaking TNF alpha trimers. |
| URI | http://hdl.handle.net/20.500.11897/438860 |
| ISSN | 2040-2503 |
| DOI | 10.1039/c5md00549c |
| Indexed | SCI(E) |
| Appears in Collections: | 生命科学学院 å å¦ä¸ å å å·¥ç¨ å¦é ¢ |
