Detection of β-amyloid peptide (1–16) and amyloid precursor protein (APP770) using spectroscopic ellipsometry and QCM techniques: A step forward towards Alzheimers disease diagnostics

Mustafa, Mohd Kamarulzaki; Nabok, Alexei; Parkinson, David K.; Tothill, Ibtisam E.; Salam, Faridah; Tsargorodskaya, A.

doi:10.1016/j.bios.2010.07.042

Cited by 51 publications

(21 citation statements)

References 24 publications

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“…This implies that the detection sensitivity of BTIRIE reaches the order of 0.1 ng/mL, which is > 10 times more sensitive than BIE. Mustafa et al (2010) exploited spectroscopic BTIRE as a highly sensitive method to detect β-amyloid peptide (Aβ-16). Monoclonal DE2 antibodies were electrostatically immobilized on a gold surface to capture Aβ-16 over a wide range of concentrations.…”

Section: Btirie Applicationsmentioning

confidence: 99%

Protein microarray biosensors based on imaging ellipsometry techniques and their applications

Niu

Jin

2011

Protein Cell

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Section: Btirie Applicationsmentioning

confidence: 99%

Protein microarray biosensors based on imaging ellipsometry techniques and their applications

Niu

Jin

2011

Protein Cell

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“…[17][18][19][20] While these techniques address the underlying molecular aspects, immunoassays involving antibodies specific to Ab bridge the gap to the clinic. [21,22] Alternatively, robust, facile and low-cost electrochemical methods are useful for probing Ab fibrilization and its inhibition. For example, the oxidation of a Tyr residue present in Ab has been exploited to monitor its aggregation in solution and on surfaces.…”

Section: Introductionmentioning

confidence: 99%

Electrochemical “Signal‐On” Reporter for Amyloid Aggregates

2011

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The synthesis and characterization of four new Ferrocene (Fc) bioconjugates, bearing a podant (Lys)-Leu-Val-Phe-Phe motif, namely the hydrophobic sequence of amyloid-β-peptides (Aβ), is reported. The Fc-peptide conjugates are characterized by a reversible redox activity and the ability to undergo hydrophobic and hydrogen bonding interactions. Biomolecular interactions between Fc-bioconjugates with Aβ(12-28) fragments were studied by circular dichroism (CD), transmission electron microscopy (TEM), and electrochemistry. All four Fc-peptides interacted favourable with Aβ(12-28) and prevented fibril formation, the extent of which depended on the length of the peptide and the nature of the C-terminal group. The aggregates obtained for the Aβ(12-28)/Fc-peptide mixtures range from short fibrils to spherical aggregates. We demonstrated that in solution the peptide sequence and peptide charge affect the biomolecular interactions. Fc-peptide interactions with immobilized Aβ(12-28)-Cys films on Au surfaces were detected by measuring the current response of the Fc redox process. The formal redox potential, E(0), at ~440 (10) mV and i(pc)/i(pa) at 0.9 were observed characteristic for the monosubstituted Fc-derivative undergoing a one-electron redox process. On the surface, methyl ester-protected Fc-peptides (1 and 3) interacted only weakly with Aβ(12-28)-Cys films, giving rise to minimal redox activity. In contrast, charged Fc-peptides (2 and 4) gave a significant electrochemical readout following the interaction with Aβ(12-28)-Cys films. Interestingly, the Fc-peptide charge dictates the surface-assisted interactions, while hydrophobic and ionic effects contribute to the overall solution behaviour of the Fc-bioconjugates with Aβ(12-28).

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“…One good candidate to detect milk adulteration is by using quartz crystal microbalance (QCM). As shown in many works, the QCM sensor has been proved to be a good immunosensor [15][16][17][18][19][20]. Commercial quartz crystal resonator with polystyrene coating has been used successfully and developed as a basis for QCM Immunosensor [21][22][23][24][25].…”

Section: Introductionmentioning

confidence: 99%

Development of QCM Biosensor with Specific Cow Milk Protein Antibody for Candidate Milk Adulteration Detection

et al. 2016

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Adulteration of goat milk is usually done using cow's milk product. Cow milk is used as it is widely available and its price is cheaper compared to goat milk. This paper shows a development of candidate tools for milk adulteration using cow milk. A quartz crystal microbalance immunosensor was developed using commercial crystal resonator and polyclonal antibody specific to cow milk protein. A specific protein at 208 KDa is found only in cow milk and does not exist in goat milk. The existence of this protein can be used as an indicator of cow milk content in a target solution. To detect the PSS 208 kDa protein, antibody specific to the PSS 208 was developed. The purified antibody was immobilized on top of the sensor surface on a polystyrene layer. The fraction of the immobilized antibody on the sensor was found at 1.5% of the given antibody. Using a static reaction cell, the developed immunosensor could detect the specific cow milk protein in buffer solution. The detection limit is 1 ppm. A linear relationship between frequency change and specific protein of cow milk concentration is found from a concentration of 1 ppm to 120 ppm.

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Detection of β-amyloid peptide (1–16) and amyloid precursor protein (APP770) using spectroscopic ellipsometry and QCM techniques: A step forward towards Alzheimers disease diagnostics

Cited by 51 publications

References 24 publications

Protein microarray biosensors based on imaging ellipsometry techniques and their applications

Protein microarray biosensors based on imaging ellipsometry techniques and their applications

Electrochemical “Signal‐On” Reporter for Amyloid Aggregates

Development of QCM Biosensor with Specific Cow Milk Protein Antibody for Candidate Milk Adulteration Detection

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