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Studies on the interactions of copper and zinc ions with β-amyloid peptides by a surface plasmon resonance biosensor.

Yao F, Zhang R, Tian H, Li X - Int J Mol Sci (2012)

Bottom Line: Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions.A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected.The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

View Article: PubMed Central - PubMed

Affiliation: College of Chemistry and Chemical Engineering, Graduate University, Chinese Academy of Sciences, Beijing, 100049, China; E-Mail: yaofuj09b@mails.gucas.ac.cn.

ABSTRACT
The aggregation of β-amyloid peptide (Aβ) into fibrils plays an important role in the pathogenesis of Alzheimer's disease (AD). Metal ions including copper and zinc are closely connected to the precipitation and toxicity of Aβ. In this study, a surface plasmon resonance (SPR) biosensor was constructed to investigate the interactions between Aβ and metal ions. Aβ peptide was immobilized on the SPR chip surface through a preformed alkanethiol self-assembled monolayer (SAM). Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions. A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected. The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

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Related in: MedlinePlus

Calibration curves for the interactions between various Zn2+ concentrations with Aβ1–28. Each value represents the mean ± standard deviation of three separate injections.
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Related In: Results  -  Collection

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f3-ijms-13-11832: Calibration curves for the interactions between various Zn2+ concentrations with Aβ1–28. Each value represents the mean ± standard deviation of three separate injections.

Mentions: The SPR angle shift is directly correlated with the Zn2+ concentration ([Zn2+]). In Figure 3, the calibration curve generated from the sensor response to a series of different Zn2+ concentrations is shown. The calibration curve contains two regions; the first is from 50 to 300 μM, and the second from 600 to 800 μM. Linear regression analysis of both regions yielded the following equations:


Studies on the interactions of copper and zinc ions with β-amyloid peptides by a surface plasmon resonance biosensor.

Yao F, Zhang R, Tian H, Li X - Int J Mol Sci (2012)

Calibration curves for the interactions between various Zn2+ concentrations with Aβ1–28. Each value represents the mean ± standard deviation of three separate injections.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3472777&req=5

f3-ijms-13-11832: Calibration curves for the interactions between various Zn2+ concentrations with Aβ1–28. Each value represents the mean ± standard deviation of three separate injections.
Mentions: The SPR angle shift is directly correlated with the Zn2+ concentration ([Zn2+]). In Figure 3, the calibration curve generated from the sensor response to a series of different Zn2+ concentrations is shown. The calibration curve contains two regions; the first is from 50 to 300 μM, and the second from 600 to 800 μM. Linear regression analysis of both regions yielded the following equations:

Bottom Line: Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions.A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected.The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

View Article: PubMed Central - PubMed

Affiliation: College of Chemistry and Chemical Engineering, Graduate University, Chinese Academy of Sciences, Beijing, 100049, China; E-Mail: yaofuj09b@mails.gucas.ac.cn.

ABSTRACT
The aggregation of β-amyloid peptide (Aβ) into fibrils plays an important role in the pathogenesis of Alzheimer's disease (AD). Metal ions including copper and zinc are closely connected to the precipitation and toxicity of Aβ. In this study, a surface plasmon resonance (SPR) biosensor was constructed to investigate the interactions between Aβ and metal ions. Aβ peptide was immobilized on the SPR chip surface through a preformed alkanethiol self-assembled monolayer (SAM). Our observations indicate that the immobilized Aβ undergoes a conformational change upon exposure to the metal ions. A difference in metal binding affinity between Aβ(1-28) and Aβ(1-42) was also detected. The results suggest that SPR is an effective method to characterize the interactions between Aβ and metal ions.

Show MeSH
Related in: MedlinePlus