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Dergiler / Dicle Üniversitesi Mühendislik Fakültesi Mühendislik Dergisi / 2021 / Cilt: 12 - Sayı: 1

Characterization of the influence of Amyloid β (1-42) By Way of ModelingSynaptic Cleft with an RC Electronic Circuit

İbrahim IŞIK
Mehmet Emin TAĞLUK
Sayfa
53–59
Yayın Tarihi
2022-10-11
DOI
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⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

These results could be linked to hypothesize thatamyloids have a common feature in structuring channel-like concentrations which are supported by theirelectrical activity as well as the rate of permeability of Calcium like cautions.

📌 3 Maddede Bu Makale

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Amaç & Hipotez:The research toward understanding the role of oligomeric amyloids in Alzheimer’s disease (AD) hasgained considerable attention in recent years.
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Temel Bulgular & Veri:As a result of the increaseof cellular calcium level, local micromechanical properties of cells can change and thus inducereorganization of cytoskeletal structures that can cause neurodegenerative disorders such as AD.Therefore, in this study we have tried to specify the effect of alteration of permittivity and permeability ofsynaptic channel as modeling synaptic cleft by an RC circuit.
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Sonuç & Katkı:These results could be linked to hypothesize thatamyloids have a common feature in structuring channel-like concentrations which are supported by theirelectrical activity as well as the rate of permeability of Calcium like cautions.
🔬Tür:Modelleme & Sayısal Simülasyon
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Alan Parametreleri

Abstract

The research toward understanding the role of oligomeric amyloids in Alzheimer’s disease (AD) hasgained considerable attention in recent years. The information obtained in this direction showed thatAmyloid Derived Diffusible Ligands (ADDLs) cause ambiguous ions movements across lipid bilayers inthe plasma membrane and consequently alter its dielectric properties such as permeability. Nevertheless,how this amyloid protein selectively alters the permeability of the cell membrane has not been noted downbecause none of the specific receptors have been identified for ADDLs binding. As a result of the increaseof cellular calcium level, local micromechanical properties of cells can change and thus inducereorganization of cytoskeletal structures that can cause neurodegenerative disorders such as AD.Therefore, in this study we have tried to specify the effect of alteration of permittivity and permeability ofsynaptic channel as modeling synaptic cleft by an RC circuit. By linking the electronic neuronal modelsthat we have previously designed with the RC cleft model, when the information transferred from oneneuron to another, the rate of error measured on the later neuron circuit with reference to the former onewas determined with respect to the rate of change of R and C values individually. It was observed that Cand R, and hence permeability of the synaptic channel do affect the communication error. It is concludedthat a healthy synaptic channel conserves optimum resistivity and capacity levels at which the inter neuronal signaling is achieved at a minimum error. These results could be linked to hypothesize thatamyloids have a common feature in structuring channel-like concentrations which are supported by theirelectrical activity as well as the rate of permeability of Calcium like cautions.

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Bu Makaleye Atıf Yap

IŞIK, İ., TAĞLUK, M. E. (2022). Characterization of the influence of Amyloid β (1-42) By Way of ModelingSynaptic Cleft with an RC Electronic Circuit. Dicle Üniversitesi Mühendislik Fakültesi Mühendislik Dergisi, Cilt: 12 - Sayı: 1, 53–59. https://ajindex.com/articles/487535

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Kaynakça (13)

  1. Gong YS, Chang L, Viola KL, Lacor PN, Lambert MP, Finch CE, Krafft GA, Klein WL., “Alzheimer’s disease-affected brain: Presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss.” Proc Natl Acad Sci U S A 2003;100:10417–10422. [PubMed: 12925731]]
  2. Sokolov Y, Ashot Kozak J, Kayed R, Chanturia A, Glabe CG, Hall JE., “Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure.” J Gen Physiol 2006;128:637–647. [PubMed: 17101816]]
  3. Green JD, Kreplak L, Goldsbury C, Blatter XL, Stolz M, Cooper GS, Seelig A, Kist-Ler J, Aebi U., “Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.”, J Mol Biol 2004;342:877–887. [PubMed: 15342243]
  4. Kayed R, Sokolov Y, Edmonds B, MacIntire TM, Milton SC, Hall JE, Glabe CG., “Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein Misfolding diseases”,. J Biol Chem. 2004, 279(45):46363-6
  5. Lin H, Bhatia R, Lal R. “Amyloid beta protein forms ion channels: implications for Alzheimer’s disease pathophysiology”. Faseb J 2001;15:2433–2444. [PubMed: 11689468]
  6. Lin H, Zhu YWJ, Lal R. “Amyloid beta protein (1–40) forms calcium-permeable, Zn2+- sensitive channel in reconstituted lipid vesicles”. Biochemistry 1999;38:11189– 11196. [PubMed: 10460176]
  7. Quist A, Doudevski I, Lin H, Azimova R, Ng D, Frangione B, Kagan B, Ghiso J, Lal R. “Amyloid ion channels: A common structural link for protein-misfolding disease”. Proc Natl Acad Sci U S A 2005;102:10427–10432. [PubMed: 16020533]
  8. Arispe N. “Architecture of the Alzheimer’s A beta P ion channel pore”. J Membr Biol 2004;197:33–48. [PubMed: 15014916]
  9. Ratnesh Lal, Hai Lin, and Arjan P. Quist, “Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm.” Biochim Biophys Acta. 2007, 1768(8): 1966– 1975. doi:10.1016/j.bbamem.2007.04.021
  10. Thomas T, Thomas G, McLendon C, Sutton T, Mullan M. “Beta amyloid mediated vasoactivity and vascular endothelial damage.” Nature 1996;380:168–171. [PubMed: 8600393]
  11. Mattson MP. “Cellular actions of betaamyloid precursor protein and its soluble and fibrillogenic derivatives.” Physiol Rev 1997;77:1081–1132. [PubMed: 9354812]
  12. Mobley DL, Cox DL, Singh RRP, Maddox MW, Longo ML. “Modeling amyloid betapeptide insertion into lipid bilayers”. Biophys J 2004;86:3585–3597. [PubMed: 15189856]
  13. Durell SR, Gu