Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+

doi:10.1007/s00775-012-0972-2

	Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+; Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+; Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+
	Zhang, Liyun 1,2; Luo, Zhaofeng 3; Zhang, Lidong 2; Jia, Liangyuan 2; Wu, Lifang1,3
	2013-02-01 ; 2013-02-01 ; 2013-02-01
发表期刊	JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY ; JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY ; JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
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.; 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.; 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.
文章类型	Article ; Article ; Article
关键词	Cu2++ Ion Cu2++ Ion Cu2++ Ion Cyclic Peptide Cyclic Peptide Cyclic Peptide Metal Sensor Metal Sensor Metal Sensor Mass Spectrometry Mass Spectrometry Mass Spectrometry
WOS标题词	Science & Technology ; Science & Technology ; Science & Technology ; Life Sciences & Biomedicine ; Life Sciences & Biomedicine ; Life Sciences & Biomedicine ; Physical Sciences ; Physical Sciences ; Physical Sciences
学科领域	离子束生物工程 ; 离子束生物工程 ; 离子束生物工程
DOI	10.1007/s00775-012-0972-2 ; 10.1007/s00775-012-0972-2 ; 10.1007/s00775-012-0972-2
关键词[WOS]	COPPER(II) COORDINATION ABILITIES ; COPPER(II) COORDINATION ABILITIES ; COPPER(II) COORDINATION ABILITIES ; BIOLOGICAL-ACTIVITY ; BIOLOGICAL-ACTIVITY ; BIOLOGICAL-ACTIVITY ; METAL-IONS ; METAL-IONS ; METAL-IONS ; MODEL PEPTIDES ; MODEL PEPTIDES ; MODEL PEPTIDES ; RING SIZE ; RING SIZE ; RING SIZE ; COMPLEXES ; COMPLEXES ; COMPLEXES ; BINDING ; BINDING ; BINDING ; PROTEIN ; PROTEIN ; PROTEIN ; CHEMISTRY ; CHEMISTRY ; CHEMISTRY ; SPECTROSCOPY ; SPECTROSCOPY ; SPECTROSCOPY
收录类别	SCI ; SCI ; SCI
语种	英语 ; 英语 ; 英语
WOS研究方向	Biochemistry & Molecular Biology ; Biochemistry & Molecular Biology ; Biochemistry & Molecular Biology ; Chemistry ; Chemistry ; Chemistry
WOS类目	Biochemistry & Molecular Biology ; Biochemistry & Molecular Biology ; Biochemistry & Molecular Biology ; Chemistry, Inorganic & Nuclear ; Chemistry, Inorganic & Nuclear ; Chemistry, Inorganic & Nuclear
WOS记录号	WOS:000314526200011 ; WOS:000314526200011 ; WOS:000314526200011
引用统计	被引频次：6[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.hfcas.ac.cn:8080/handle/334002/10496
专题	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+, Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+, Interactions of disulfide-constrained cyclic tetrapeptides with Cu2+[J]. JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY,2013, 2013, 2013,18, 18, 18(2):277-286, 277-286, 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.

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