Crocetin inhibits beta-amyloid fibrillization and stabilizes beta-amyloid oligomers

Joon Ho Ahn, Yang Hu, Michael Hernandez, Jin Kim

Research output: Contribution to journalArticle

Abstract

Aggregation of a peptide, beta-amyloid (Aβ), is a hallmark molecular process found in Alzheimer's disease (AD). During Aβ aggregation, oligomeric and fibrillar Aβ are formed, and these molecular self-assembly steps are implicated in generation of toxic effects in AD. Crocetin is a natural carotenoid dicarboxyl acid displaying various pharmaceutical effects and may be co-localized with Aβ mediated by human serum albumin. In the study presented here, we examined the effects of crocetin on Aβ aggregation in three different molecular pathways. Our results demonstrate that crocetin inhibited Aβ fibril formation and destabilized pre-formed Aβ fibrils. Moreover, crocetin caused stabilization of Aβ oligomers and prevented their conversion into Aβ fibrils. Our study reveals potential pathological and pharmaceutical implication of crocetin in AD and suggests possible application of crocetin for currently limited structural studies on unstable Aβ oligomers.

Original languageEnglish (US)
Pages (from-to)79-83
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume414
Issue number1
DOIs
StatePublished - Oct 14 2011

Fingerprint

Oligomers
Amyloid
Alzheimer Disease
Agglomeration
Cohort Effect
Poisons
Amyloid beta-Peptides
Carotenoids
Serum Albumin
Pharmaceutical Preparations
Self assembly
crocetin
Stabilization
Acids

Keywords

  • Beta-amyloid
  • Crocetin
  • Fibril
  • Oligomer
  • Protein aggregation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crocetin inhibits beta-amyloid fibrillization and stabilizes beta-amyloid oligomers. / Ahn, Joon Ho; Hu, Yang; Hernandez, Michael; Kim, Jin.

In: Biochemical and Biophysical Research Communications, Vol. 414, No. 1, 14.10.2011, p. 79-83.

Research output: Contribution to journalArticle

@article{a363685bda044a6e9aee50b939708d05,
title = "Crocetin inhibits beta-amyloid fibrillization and stabilizes beta-amyloid oligomers",
abstract = "Aggregation of a peptide, beta-amyloid (Aβ), is a hallmark molecular process found in Alzheimer's disease (AD). During Aβ aggregation, oligomeric and fibrillar Aβ are formed, and these molecular self-assembly steps are implicated in generation of toxic effects in AD. Crocetin is a natural carotenoid dicarboxyl acid displaying various pharmaceutical effects and may be co-localized with Aβ mediated by human serum albumin. In the study presented here, we examined the effects of crocetin on Aβ aggregation in three different molecular pathways. Our results demonstrate that crocetin inhibited Aβ fibril formation and destabilized pre-formed Aβ fibrils. Moreover, crocetin caused stabilization of Aβ oligomers and prevented their conversion into Aβ fibrils. Our study reveals potential pathological and pharmaceutical implication of crocetin in AD and suggests possible application of crocetin for currently limited structural studies on unstable Aβ oligomers.",
keywords = "Beta-amyloid, Crocetin, Fibril, Oligomer, Protein aggregation",
author = "Ahn, {Joon Ho} and Yang Hu and Michael Hernandez and Jin Kim",
year = "2011",
month = "10",
day = "14",
doi = "10.1016/j.bbrc.2011.09.025",
language = "English (US)",
volume = "414",
pages = "79--83",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Crocetin inhibits beta-amyloid fibrillization and stabilizes beta-amyloid oligomers

AU - Ahn, Joon Ho

AU - Hu, Yang

AU - Hernandez, Michael

AU - Kim, Jin

PY - 2011/10/14

Y1 - 2011/10/14

N2 - Aggregation of a peptide, beta-amyloid (Aβ), is a hallmark molecular process found in Alzheimer's disease (AD). During Aβ aggregation, oligomeric and fibrillar Aβ are formed, and these molecular self-assembly steps are implicated in generation of toxic effects in AD. Crocetin is a natural carotenoid dicarboxyl acid displaying various pharmaceutical effects and may be co-localized with Aβ mediated by human serum albumin. In the study presented here, we examined the effects of crocetin on Aβ aggregation in three different molecular pathways. Our results demonstrate that crocetin inhibited Aβ fibril formation and destabilized pre-formed Aβ fibrils. Moreover, crocetin caused stabilization of Aβ oligomers and prevented their conversion into Aβ fibrils. Our study reveals potential pathological and pharmaceutical implication of crocetin in AD and suggests possible application of crocetin for currently limited structural studies on unstable Aβ oligomers.

AB - Aggregation of a peptide, beta-amyloid (Aβ), is a hallmark molecular process found in Alzheimer's disease (AD). During Aβ aggregation, oligomeric and fibrillar Aβ are formed, and these molecular self-assembly steps are implicated in generation of toxic effects in AD. Crocetin is a natural carotenoid dicarboxyl acid displaying various pharmaceutical effects and may be co-localized with Aβ mediated by human serum albumin. In the study presented here, we examined the effects of crocetin on Aβ aggregation in three different molecular pathways. Our results demonstrate that crocetin inhibited Aβ fibril formation and destabilized pre-formed Aβ fibrils. Moreover, crocetin caused stabilization of Aβ oligomers and prevented their conversion into Aβ fibrils. Our study reveals potential pathological and pharmaceutical implication of crocetin in AD and suggests possible application of crocetin for currently limited structural studies on unstable Aβ oligomers.

KW - Beta-amyloid

KW - Crocetin

KW - Fibril

KW - Oligomer

KW - Protein aggregation

UR - http://www.scopus.com/inward/record.url?scp=80054071097&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80054071097&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2011.09.025

DO - 10.1016/j.bbrc.2011.09.025

M3 - Article

VL - 414

SP - 79

EP - 83

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -