Acceleration of deposition of Aβ1−40 peptide on ultrasonically formed Aβ1−42 nucleus studied by wireless quartz-crystal-microbalance biosensor

• Published in: Biosensors & bioelectronics Vol. 40; no. 1; pp. 200 - 205
• Main Authors: Ogi, Hirotsugu, Fukushima, Masahiko, Uesugi, Kentaro, Yagi, Hisashi, Goto, Yuji, Hirao, Masahiko
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Kidlington Elsevier B.V 15.02.2013; Elsevier
• Subjects: Biological and medical sciences; Biosensors; Biotechnology; Deposition rate; formula omitted; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Oligomer; QCM; Ultrasonication; Various methods and equipments; Aβ; Ultrasonication; QCM; Deposition rate; Oligomer; Peptides; Biosensor; Crystals; Ultrasound; Deposition; Quartz microbalance
• ISSN: 0956-5663; 1873-4235
• DOI: 10.1016/j.bios.2012.07.019

High-frequency (∼ 55MHz) wireless quartz-crystal microbalance biosensor was used for studying heterogeneous deposition behavior of Aβ1−40 peptide on Aβ1−42 nuclei, which were grown under the stirring agitation and 200-kHz ultrasonication at pH 2.2, 4.6, and 7.4. The deposition reaction was monitored over 40h, and the deposition rate was deduced. Among the agitation nuclei, the maximum deposition rate was observed on the nucleus grown at pH 4.6. However, ultrasonication nucleus grown at pH 7.4 produced much larger deposition rate, despite the same β-sheet concentration. This result indicates that local structural modulation is caused in the nucleus by ultrasonication, which adsorbs the Aβ peptide more actively than other nuclei. The resultant deposits clearly show oligomeric structure. ► We discovered anomalously high deposition rate of Alzheimer's disease peptides. ► Aβ1−40 monomer accumulates on ultrasonically formed Aβ1−42 seeds. ► Homebuilt multichannel QCM was used for long-time deposition monitoring. ► Deposited structure is clearly oligomeric. ► Discovered deposition system can be used for the drug development.