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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

The sensorgram for the interactions between Zn2+ ions and Aβ1–42. Various concentrations (50, 100, 300, 400, 500 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Zn2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–42 and when the flow of metal ions ends, respectively.
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f5-ijms-13-11832: The sensorgram for the interactions between Zn2+ ions and Aβ1–42. Various concentrations (50, 100, 300, 400, 500 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Zn2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–42 and when the flow of metal ions ends, respectively.

Mentions: Figure 5 depicts SPR sensorgrams obtained from the sensor response to various Zn2+ concentrations. In contrast to the calibration curve of the Zn2+ interactions with Aβ1–28 that contains two regions, the calibration plot of the Zn interactions with Aβ1–42 only contains one region; the linear regression equation is as follows:


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)

The sensorgram for the interactions between Zn2+ ions and Aβ1–42. Various concentrations (50, 100, 300, 400, 500 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Zn2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–42 and when the flow of metal ions ends, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f5-ijms-13-11832: The sensorgram for the interactions between Zn2+ ions and Aβ1–42. Various concentrations (50, 100, 300, 400, 500 and 800 μM, from top to bottom) of Zn2+ ions were injected onto the Aβ1–42 sensorchip. The inset shows the calibration curve for the interactions between various concentrations of Zn2+ with Aβ1–42. Each value represents the mean ± standard deviation of three separate injections. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1–42 and when the flow of metal ions ends, respectively.
Mentions: Figure 5 depicts SPR sensorgrams obtained from the sensor response to various Zn2+ concentrations. In contrast to the calibration curve of the Zn2+ interactions with Aβ1–28 that contains two regions, the calibration plot of the Zn interactions with Aβ1–42 only contains one region; the linear regression equation is as follows:

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