Current status of PET-imaging probes of β-amyloid plaques

Jaehyung Koo, Youngjoo Byun

Research output: Contribution to journalArticle

Abstract

Alzheimer's disease (AD) is the most common form of dementia and is characterized by progressive cognitive decline and memory loss. One of pathological hallmarks of AD is the accumulation and deposition of β-amyloid (Aβ) plaques which is a potential target for the early diagnosis of AD. Positron emission tomography (PET), a sensitive radionuclide imaging technique, has provided opportunities to detect Aβ plaques of AD. PET-imaging probes of Aβ plaques have been extensively developed during the last decade. [18F]Florbetapir, the 18F-labeled PET-imaging probe of Aβ plaques, was recently approved by US Food and Drug Administration. A number of follow-on PET-imaging probes are currently being developed in academia and pharmaceutical companies. This article will discuss the recent development of PET-imaging probes from [11C]PIB to [ 18F]Florbetapir, which are in clinic trials, and several follow-on probes in preclinical stage.

Original languageEnglish (US)
Pages (from-to)1178-1184
Number of pages7
JournalArchives of Pharmacal Research
Volume36
Issue number10
DOIs
StatePublished - Oct 2013
Externally publishedYes

Fingerprint

Positron emission tomography
Amyloid Plaques
Amyloid
Positron-Emission Tomography
Alzheimer Disease
Imaging techniques
Memory Disorders
United States Food and Drug Administration
Radioisotopes
Radionuclide Imaging
Dementia
Early Diagnosis
Data storage equipment
Pharmaceutical Preparations
Industry

Keywords

  • Alzheimer's disease
  • Amyloid plaques
  • PET-imaging

ASJC Scopus subject areas

  • Drug Discovery
  • Molecular Medicine
  • Organic Chemistry

Cite this

Current status of PET-imaging probes of β-amyloid plaques. / Koo, Jaehyung; Byun, Youngjoo.

In: Archives of Pharmacal Research, Vol. 36, No. 10, 10.2013, p. 1178-1184.

Research output: Contribution to journalArticle

Koo, Jaehyung ; Byun, Youngjoo. / Current status of PET-imaging probes of β-amyloid plaques. In: Archives of Pharmacal Research. 2013 ; Vol. 36, No. 10. pp. 1178-1184.
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