Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus
文献类型：期刊论文
| 作者 | Han, YH; Huang, FJ; Jiang, H; Liu, L; Wang, Q; Wang, YF; Shao, XX; Chi, CW; Du, WH; Wang, CG |
| 刊名 | FEBS JOURNAL
 |
| 出版日期 | 2008 |
| 卷号 | 275期号:9页码:1976-1987 |
| 关键词 | conomarphin Conus marmoreus D-phe M-superfamily NMR structure |
| 通讯作者 | Wang, CG (reprint author), Tongji Univ, Inst Prot Res, 1239 Siping Rd, Shanghai 200092, Peoples R China.,whdu@chem.ruc.edu.cn ; chunguangwang@mail.tongji.edu.cn |
| 英文摘要 | Cone snails, a group of gastropod animals that inhabit tropical seas, are capable of producing a mixture of peptide neurotoxins, namely conotoxins, for defense and predation. Conotoxins are mainly disulfide-rich short peptides that act on different ion channels, neurotransmitter receptors, or transporters in the nervous system. They exhibit highly diverse compositions, structures, and biological functions. In this work, a novel Cys-free 15-residue conopeptide from Conus marmoreus was purified and designated as conomarphin. Conomarphin is unique because of its D-configuration Phe at the third residue from the C-terminus, which was identified using HPLC by comparing native conomarphin fragments and the corresponding synthetic peptides cleaved by different proteases. Surprisingly, the cDNA-encoded precursor of conomarphin was found to share the conserved signal peptide with other M-superfamily conotoxins, clearly indicating that conomarphin should belong to the M-superfamily, although conomarphin shares no homology with other six-Cys-containing M-superfamily conotoxins. Furthermore, NMR spectroscopy experiments established that conomarphin adopts a well-defined structure in solution, with a tight loop in the middle of the peptide and a short 3(10)-helix at the C-terminus. By contrast, no loop in L-Phe13-conomarphin was found, which suggests that D-Phe13 is essential for the structure of conomarphin. In conclusion, conomarphin may represent a new conotoxin family, whose biological activity remains to be identified. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | FUNNEL-WEB SPIDER ; 3-DIMENSIONAL STRUCTURE ; CONOTOXIN SUPERFAMILY ; CONTAINING CONTRYPHAN ; EXCITATORY PEPTIDE ; DISULFIDE LINKAGE ; CHANNEL MODULATOR ; SODIUM-CHANNEL ; PLATYPUS VENOM ; D-TRYPTOPHAN |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000255137800004 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1438]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Han, YH,Huang, FJ,Jiang, H,et al. Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus[J]. FEBS JOURNAL,2008,275(9):1976-1987. |
| APA | Han, YH.,Huang, FJ.,Jiang, H.,Liu, L.,Wang, Q.,...&Wang, CG.(2008).Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus.FEBS JOURNAL,275(9),1976-1987. |
| MLA | Han, YH,et al."Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus".FEBS JOURNAL 275.9(2008):1976-1987. |
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