Development of liquid crystal biosensor for the detection of amyloid beta-42 levels associated with Alzheimer's disease

KEMİKLİOĞLU E., Tuncgovde E. B., Ozsarlak-Sozer G.

Journal of Bioscience and Bioengineering, cilt.132, sa.1, ss.88-94, 2021 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 132 Sayı: 1
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1016/j.jbiosc.2021.03.016
  • Dergi Adı: Journal of Bioscience and Bioengineering
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, PASCAL, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Chimica, Compendex, EMBASE, Environment Index, Food Science & Technology Abstracts, INSPEC, MEDLINE, Veterinary Science Database
  • Sayfa Sayıları: ss.88-94
  • Anahtar Kelimeler: Amyloid beta-42, Apolipoprotein E4, DMOAP coating, Liquid crystal, Liquid crystal biosensor
  • Manisa Celal Bayar Üniversitesi Adresli: Evet

Özet

This study represents the development of a biosensor which is based on the liquid crystal (LC) orientation as a function of the peptide concentration to detect an amyloid-beta-42 (Aβ42) antibody–antigen binding events. The Aβ42 peptide binds to the Aβ42 antibody forming an immunocomplex which is immobilized on the Dimethyloctadecyl[3-(trimethoxysilyl)propyl] ammonium chloride (DMOAP) coated surface. The disturbed orientation of LCs as a result of the binding of the formed immunocomplex was observed using the polarized optical microscope (POM) as a function of decreasing Aβ42 peptide concentration from 1000 to 1 pg/ml. The concentration, as low as 1 pg/ml of Aβ42 peptide was able to be successfully detected in our system. Apolipoprotein E4 (ApoE4), that specifically bound to the Aβ42 peptide, was added into the system and a remarkable change in reflection spectra of samples was observed with increasing Aβ42 peptide concentration. The concentration of ApoE4 protein was detected in the range of 0.1–30 nM by this system due to the interaction between the two proteins.