Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes

Toshinori Shimanouchi, Ryo Onishi, Nachi Kitaura, Hiroshi Umakoshi, Ryoichi Kuboi

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Amyloid β protein (Aβ) from Alzheimer's disease formed fibrillar aggregates and their morphology depended on oxidized and negatively charged liposomes. The morphology of fibrillar aggregates was affected by Cu 2+, together with their growth kinetics. This is because Cu 2+ inhibited the nucleation step in the formation of amyloid Aβ fibrillar aggregates by forming Aβ/Cu complex inactive to the growth of fibrillar aggregates. In addition, this is probably because Cu 2+ affected the fibrillar aggregate formed on the surface of liposomes. These findings would give a better understanding of the formation mechanism of amyloid fibrils on biomembranes.

Original languageEnglish
Pages (from-to)611-615
Number of pages5
JournalJournal of Bioscience and Bioengineering
Volume112
Issue number6
DOIs
Publication statusPublished - Dec 2011
Externally publishedYes

Fingerprint

Liposomes
Amyloid
Copper
Serum Amyloid A Protein
Growth
Alzheimer Disease
Growth kinetics
Nucleation

Keywords

  • Amyloid β protein
  • Copper ion
  • Liposome
  • Morphology

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes. / Shimanouchi, Toshinori; Onishi, Ryo; Kitaura, Nachi; Umakoshi, Hiroshi; Kuboi, Ryoichi.

In: Journal of Bioscience and Bioengineering, Vol. 112, No. 6, 12.2011, p. 611-615.

Research output: Contribution to journalArticle

Shimanouchi, Toshinori ; Onishi, Ryo ; Kitaura, Nachi ; Umakoshi, Hiroshi ; Kuboi, Ryoichi. / Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes. In: Journal of Bioscience and Bioengineering. 2011 ; Vol. 112, No. 6. pp. 611-615.
@article{2dc62aca53a74a7c8cf8613a50d52db3,
title = "Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes",
abstract = "Amyloid β protein (Aβ) from Alzheimer's disease formed fibrillar aggregates and their morphology depended on oxidized and negatively charged liposomes. The morphology of fibrillar aggregates was affected by Cu 2+, together with their growth kinetics. This is because Cu 2+ inhibited the nucleation step in the formation of amyloid Aβ fibrillar aggregates by forming Aβ/Cu complex inactive to the growth of fibrillar aggregates. In addition, this is probably because Cu 2+ affected the fibrillar aggregate formed on the surface of liposomes. These findings would give a better understanding of the formation mechanism of amyloid fibrils on biomembranes.",
keywords = "Amyloid β protein, Copper ion, Liposome, Morphology",
author = "Toshinori Shimanouchi and Ryo Onishi and Nachi Kitaura and Hiroshi Umakoshi and Ryoichi Kuboi",
year = "2011",
month = "12",
doi = "10.1016/j.jbiosc.2011.08.015",
language = "English",
volume = "112",
pages = "611--615",
journal = "Journal of Bioscience and Bioengineering",
issn = "1389-1723",
publisher = "The Society for Biotechnology, Japan",
number = "6",

}

TY - JOUR

T1 - Copper-mediated growth of amyloid β fibrils in the presence of oxidized and negatively charged liposomes

AU - Shimanouchi, Toshinori

AU - Onishi, Ryo

AU - Kitaura, Nachi

AU - Umakoshi, Hiroshi

AU - Kuboi, Ryoichi

PY - 2011/12

Y1 - 2011/12

N2 - Amyloid β protein (Aβ) from Alzheimer's disease formed fibrillar aggregates and their morphology depended on oxidized and negatively charged liposomes. The morphology of fibrillar aggregates was affected by Cu 2+, together with their growth kinetics. This is because Cu 2+ inhibited the nucleation step in the formation of amyloid Aβ fibrillar aggregates by forming Aβ/Cu complex inactive to the growth of fibrillar aggregates. In addition, this is probably because Cu 2+ affected the fibrillar aggregate formed on the surface of liposomes. These findings would give a better understanding of the formation mechanism of amyloid fibrils on biomembranes.

AB - Amyloid β protein (Aβ) from Alzheimer's disease formed fibrillar aggregates and their morphology depended on oxidized and negatively charged liposomes. The morphology of fibrillar aggregates was affected by Cu 2+, together with their growth kinetics. This is because Cu 2+ inhibited the nucleation step in the formation of amyloid Aβ fibrillar aggregates by forming Aβ/Cu complex inactive to the growth of fibrillar aggregates. In addition, this is probably because Cu 2+ affected the fibrillar aggregate formed on the surface of liposomes. These findings would give a better understanding of the formation mechanism of amyloid fibrils on biomembranes.

KW - Amyloid β protein

KW - Copper ion

KW - Liposome

KW - Morphology

UR - http://www.scopus.com/inward/record.url?scp=83555177329&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=83555177329&partnerID=8YFLogxK

U2 - 10.1016/j.jbiosc.2011.08.015

DO - 10.1016/j.jbiosc.2011.08.015

M3 - Article

C2 - 21917513

AN - SCOPUS:83555177329

VL - 112

SP - 611

EP - 615

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

SN - 1389-1723

IS - 6

ER -