Fluorescence and molecular dynamics studies of the acetylcholine receptor gamma M4 transmembrane peptide in reconstituted systems
文献类型：期刊论文
| 作者 | Antollini, SS; Xu, YC ; Jiang, HL; Barrantes, FJ
|
| 刊名 | MOLECULAR MEMBRANE BIOLOGY
 |
| 出版日期 | 2005-11 |
| 卷号 | 22期号:6页码:471-484 |
| 关键词 | acetylcholine receptor fluorescence molecular modeling protein-lipid interactions secondary structure |
| ISSN号 | 0968-7688 |
| DOI | 10.1080/09687860500367915 |
| 文献子类 | Article |
| 英文摘要 | A combination of fluorescence spectroscopy and molecular dynamics ( MD) is applied to assess the conformational dynamics of a peptide making up the outermost ring of the nicotinic acetylcholine receptor ( AChR) transmembrane region and the effect of membrane thickness and cholesterol on the hydrophobic matching of this peptide. The fluorescence studies exploit the intrinsic fluorescence of the only tryptophan residue in a synthetic peptide corresponding to the fourth transmembrane domain of the AChR gamma subunit (gamma M4-Trp(6)) reconstituted in lipid bilayers of varying thickness, and combine this information with quenching studies using depth-sensitive phosphatidylcholine spin-labeled probes and acrylamide, polarization of fluorescence, and generalized polarization of Laurdan. A direct correlation was found between bilayer width and the depth of insertion of Trp(6). We further extend our recent MD study of the conformational dynamics of the AChR channel to focus on the crosstalk between M4 and the lipid-belt region. The isolated gamma M-4 peptide is shown to possess considerable orientational flexibility while maintaining a linear alpha-helical structure, and to vary its tilt depending on bilayer width and cholesterol (Chol) content. MD studies also show that gamma M4 also establishes contacts with the other TM peptides on its inner face, stabilizing a shorter TM length that is still highly sensitive to the lipid environment. In the native membrane the topology of the M4 ring is likely to exhibit a similar behavior, dynamically modifying its tilt to match the hydrophobic thickness of the bilayer. |
| WOS关键词 | NICOTINIC ACETYLCHOLINE-RECEPTOR ; MEMBRANE-LIPID-COMPOSITION ; ION-CHANNEL FUNCTION ; CHAIN FATTY-ACIDS ; TORPEDO-CALIFORNICA ; BILAYER THICKNESS ; TRYPTOPHAN SUBSTITUTIONS ; HYDROPHOBIC MISMATCH ; BIOLOGICAL-MEMBRANES ; LAURDAN FLUORESCENCE |
| WOS研究方向 | Biochemistry & Molecular Biology ; Cell Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000234127000002 |
| 出版者 | TAYLOR & FRANCIS LTD |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/273786]  |
| 专题 | 新药研究国家重点实验室 中科院受体结构与功能重点实验室 |
| 通讯作者 | Barrantes, FJ |
| 作者单位 | 1.Inst Invest Bioquim, UNESCO Chair Biophys & Mol Neurobiol, RA-8000 Bahia Blanca, Buenos Aires, Argentina 2.UNESCO Chair Biophys & Mol Neurobiol, RA-8000 Bahia Blanca, Buenos Aires, Argentina 3.Shanghai Inst Biol Sci, Ctr Drug Discovery & Design, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai, Peoples R China 4.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China |
| 推荐引用方式 GB/T 7714 | Antollini, SS,Xu, YC,Jiang, HL,et al. Fluorescence and molecular dynamics studies of the acetylcholine receptor gamma M4 transmembrane peptide in reconstituted systems[J]. MOLECULAR MEMBRANE BIOLOGY,2005,22(6):471-484. |
| APA | Antollini, SS,Xu, YC,Jiang, HL,&Barrantes, FJ.(2005).Fluorescence and molecular dynamics studies of the acetylcholine receptor gamma M4 transmembrane peptide in reconstituted systems.MOLECULAR MEMBRANE BIOLOGY,22(6),471-484. |
| MLA | Antollini, SS,et al."Fluorescence and molecular dynamics studies of the acetylcholine receptor gamma M4 transmembrane peptide in reconstituted systems".MOLECULAR MEMBRANE BIOLOGY 22.6(2005):471-484. |
入库方式： OAI收割
来源：上海药物研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。