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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 of a 200 μM Zn2+ ion solution flowing over the surface plasmon resonance (SPR) sensor chip with (a) and without (b) immobilized β-amyloid peptides (Aβ1–28) peptides. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1-28 and when the flowing of metal ions ends, respectively.
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f1-ijms-13-11832: The sensorgram of a 200 μM Zn2+ ion solution flowing over the surface plasmon resonance (SPR) sensor chip with (a) and without (b) immobilized β-amyloid peptides (Aβ1–28) peptides. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1-28 and when the flowing of metal ions ends, respectively.

Mentions: The successful immobilization of the Aβ peptide on the sensor chip surface was tested by injecting a Zn2+ ion solution into the flow chamber and pumping it across the Aβ-immobilized sensing surface. In our experiment, the sample loop volume is 20 μL, the flowing rate is 10 μL/min, so that the Zn2+ ions start to flow onto the immobilized Aβ1–28 at about 80 s, the flowing of metal ions ends at about 200 s; the difference in the baseline SPR angles before and after the Zn2+ ion solution injection (termed as the SPR dip shift Δθ) is approximately 0.00246° (Figure 1a), considering the sophisticated interaction between Aβ peptide and metal ions, the detection of the SPR dip shift Δθ is selected at 550 s.


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 of a 200 μM Zn2+ ion solution flowing over the surface plasmon resonance (SPR) sensor chip with (a) and without (b) immobilized β-amyloid peptides (Aβ1–28) peptides. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1-28 and when the flowing 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

f1-ijms-13-11832: The sensorgram of a 200 μM Zn2+ ion solution flowing over the surface plasmon resonance (SPR) sensor chip with (a) and without (b) immobilized β-amyloid peptides (Aβ1–28) peptides. Arrows indicate Zn2+ ions starting to flow onto immobilized Aβ1-28 and when the flowing of metal ions ends, respectively.
Mentions: The successful immobilization of the Aβ peptide on the sensor chip surface was tested by injecting a Zn2+ ion solution into the flow chamber and pumping it across the Aβ-immobilized sensing surface. In our experiment, the sample loop volume is 20 μL, the flowing rate is 10 μL/min, so that the Zn2+ ions start to flow onto the immobilized Aβ1–28 at about 80 s, the flowing of metal ions ends at about 200 s; the difference in the baseline SPR angles before and after the Zn2+ ion solution injection (termed as the SPR dip shift Δθ) is approximately 0.00246° (Figure 1a), considering the sophisticated interaction between Aβ peptide and metal ions, the detection of the SPR dip shift Δθ is selected at 550 s.

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