Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+
文献类型：期刊论文
| 作者 | Zhang, Liyun1,2; Luo, Zhaofeng3; Zhang, Lidong2; Jia, Liangyuan2; Wu, Lifang1,3
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| 刊名 | journal of biological inorganic chemistry
 |
| 出版日期 | 2013-02-01 |
| 卷号 | 18期号:2页码:277-286 |
| 关键词 | Cu2+ ion Cyclic peptide Metal sensor Mass spectrometry |
| 英文摘要 | the purpose of this work is to characterize the interactions of two disulfide-constrained cyclic tetrapeptides [c(ac-cys-pro-phe-cys-nh2), ss1; c(ac-cys-pro-gly-cys-nh2), ss2] with cu2+ ions in order to facilitate the design of cyclic peptides as sensors for metal ions. the cu2+-peptide complex cations at m/z 569.1315 for cu2+-ss1 and m/z 479.0815 for cu2+-ss2 were detected by mass spectrometry. the gas-phase fragmentation of the cu2+-peptide complexes was studied by collision-induced dissociation and suggests the atoms involved in the coordination. cu2+ ion binds to a single ss1 or ss2 with k (d(app)) of 0.57 +/- a 0.02 and 0.55 +/- a 0.01 mu m, respectively. isothermal titration calorimetry data indicate both enthalpic and entropic contributions for the binding of cu2+ ion to ss1 and ss2. the characteristic wavenumber of 947 cm(-1) and the changes at 1,664 and 1,530 cm(-1) in the infrared spectrum suggest that the sulfydryl of cysteine, the carbonyl group, and amide ii are involved in the coordination of cu2+. the x-ray absorption near-edge structure signal from the cu2+-peptide complex corresponds to the four-coordination structure. the extended x-ray absorption fine structure and electron paramagnetic resonance results demonstrate the cu2+ ion is in an s/n/2o coordination environment, and is a distinct type ii copper center. theoretical calculations further demonstrate that cu2+ ion binds to ss1 or ss2 in a slightly distorted tetragonal geometry with an s/n/2o environment and the minimum potential energy. |
| WOS标题词 | science & technology ; life sciences & biomedicine ; physical sciences |
| 学科主题 | 离子束生物工程 |
| 类目[WOS] | biochemistry & molecular biology ; chemistry, inorganic & nuclear |
| 研究领域[WOS] | biochemistry & molecular biology ; chemistry |
| 关键词[WOS] | copper(ii) coordination abilities ; biological-activity ; metal-ions ; model peptides ; ring size ; complexes ; binding ; protein ; chemistry ; spectroscopy |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000314526200011 |
| 公开日期 | 2013-08-29 |
| 源URL | [http://ir.hfcas.ac.cn/handle/334002/10496]  |
| 专题 | 合肥物质科学研究院_技术生物与农业工程研究所 |
| 作者单位 | 1.Chinese Acad Sci, Hefei Inst Phys Sci, Hefei 230031, Anhui, Peoples R China 2.Univ Sci & Technol China, Natl Synchrotron Radiat Lab, Hefei 230029, Anhui, Peoples R China 3.Univ Sci & Technol China, Sch Life Sci, Hefei 230027, Anhui, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, Liyun,Luo, Zhaofeng,Zhang, Lidong,et al. Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+[J]. journal of biological inorganic chemistry,2013,18(2):277-286. |
| APA | Zhang, Liyun,Luo, Zhaofeng,Zhang, Lidong,Jia, Liangyuan,&Wu, Lifang.(2013).Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+.journal of biological inorganic chemistry,18(2),277-286. |
| MLA | Zhang, Liyun,et al."Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+".journal of biological inorganic chemistry 18.2(2013):277-286. |
入库方式： OAI收割
来源：合肥物质科学研究院
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