A quadrupolar two-photon fluorescent probe for in vivo imaging of amyloid-β plaques

Heo, Cheol Ho; Sarkar, Avik; Baik, Sung-Hoon; Jung, Tae Sung; Kim, Jeong Jin; Kang, Hyuk; Mook‐Jung, Inhee; Kim, Hwan Myung

doi:10.1039/c6sc00355a

Cited by 53 publications

(36 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The first is that the lack of the highly organized smooth muscles cells in veins and venules result in less substrates for Aβ deposition and, secondly, monocytes that exclusively adhere to veins might clear Aβ as it deposits along the venular walls [4,27,39]. In addition to the preclinical models discussed above, there are reports that do not distinguish between arteries and veins [60][61][62][63][64], or exclusively report of CAA in arteries [65,66]. Therefore, the present findings in this section address the need for characterization of all cerebral vessels to accurately gain a comprehensive understanding of both arterial and venous CAA.…”

Section: Preclinical Modelsmentioning

confidence: 99%

Potential Role of Venular Amyloid in Alzheimer’s Disease Pathogenesis

Morrone

Bishay

McLaurin

2020

IJMS

View full text Add to dashboard Cite

Insurmountable evidence has demonstrated a strong association between Alzheimer’s disease (AD) and cerebral amyloid angiopathy (CAA), along with various other cerebrovascular diseases. One form of CAA, which is the accumulation of amyloid-beta peptides (Aβ) along cerebral vessel walls, impairs perivascular drainage pathways and contributes to cerebrovascular dysfunction in AD. To date, CAA research has been primarily focused on arterial Aβ, while the accumulation of Aβ in veins and venules were to a lesser extent. In this review, we describe preclinical models and clinical studies supporting the presence of venular amyloid and potential downstream pathological mechanisms that affect the cerebrovasculature in AD. Venous collagenosis, impaired cerebrovascular pulsatility, and enlarged perivascular spaces are exacerbated by venular amyloid and increase Aβ deposition, potentially through impaired perivascular clearance. Gaining a comprehensive understanding of the mechanisms involved in venular Aβ deposition and associated pathologies will give insight to how CAA contributes to AD and its association with AD-related cerebrovascular disease. Lastly, we suggest that special consideration should be made to develop Aβ-targeted therapeutics that remove vascular amyloid and address cerebrovascular dysfunction in AD.

show abstract

Section: Preclinical Modelsmentioning

confidence: 99%

Potential Role of Venular Amyloid in Alzheimer’s Disease Pathogenesis

Morrone

Bishay

McLaurin

2020

IJMS

View full text Add to dashboard Cite

show abstract

“…Fluorescence-based imaging has emerged as an increasingly important technique for monitoring diseases, 9,10 and possesses several advantages, including lower cost, no exposure to radioactivity, availability and ease of operation. 11,12 Even though there are a variety of fluorescent probes for detecting Aβ aggregates, [13][14][15][16][17][18][19] fluorescent probes that can specifically distinguish Aβ oligomers from Aβ fibrils are rare. Ran et al reported a fluorescent probe, CRANAD-58, which exhibited a significant increase in fluorescence intensity upon mixing with Aβ monomers and oligomers.…”

Section: Spiropyran-based Fluorescent Probe For Specific Detection Ofmentioning

confidence: 99%

A spiropyran-based fluorescent probe for the specific detection of β-amyloid peptide oligomers in Alzheimer's disease

Sun

Wei

et al. 2016

Chem. Commun.

View full text Add to dashboard Cite

show abstract

“…A potential route to identify efficient two-photon sensors for β-amyloid imaging is to explore the two-photon properties of the dyes that have already shown some success in this aspect. Up to now, plenty of fluorescent probes with multiple chemical structures have been synthesized and experimentally applied to detect the β-amyloid plaques in vivo, such as PAD-1, DCIP-1, and BAP-1 with donor-acceptor architecture [16][17][18], and QAD1, DADNIR-2, and CRANAD-3 with donor-acceptor-donor architecture [19][20][21]. Due to some correlations between the donor-π-acceptor structural compounds and their optical properties that have already been established [22,23], we choose molecules with the N,N-dimethylamino group as the donor and dicyano group as the acceptor to study their possibility to be two-photon fluorescent probes for detecting β-amyloid.…”

Section: Introductionmentioning

confidence: 99%

Sensing Performance Investigations on Two-Photon Fluorescent Probes for Detecting β-Amyloid in Alzheimer’s Disease

Zhang

Luan

et al. 2020

Sensors

View full text Add to dashboard Cite

Alzheimer’s disease (AD) is one of the most common forms of senile disease. In recent years, the incidence of AD has been increasing significantly with the acceleration of the aging process of the global population. However, current clinical drugs can only alleviate the symptoms of AD patients without healing the disease fundamentally. Therefore, it is of great significance to develop an effective small molecule diagnostic reagent for the early diagnosis of AD. In this paper, we employ an integrated approach, including molecular docking simulation and quantum mechanics/molecular mechanics calculation, to investigate the sensing performance of a series of donor–acceptor structural probes for the marker protein of AD (β-amyloid). Results show that the probes display evident fluorescence enhancement when bound to the β-amyloid, suggesting the effect of the environment on the molecular properties. Especially, the two-photon absorption cross-section of the probes increase drastically in the β-amyloid compared to that in vacuum, which results from the larger electron delocalization and dipole moment in the fibrillary-like environment. Thus, one can propose that the studied probes are capable of application in two-photon fluorescent imaging, particularly those containing naphthalene rings as the donor or with a longer spacer group. Our calculations elucidate the experimental measurements reasonably, and further establish possible structure–property relationships that can be used to design novel biocompatible two-photon fluorescent probes for the diagnosis of Alzheimer’s.

show abstract

A quadrupolar two-photon fluorescent probe for in vivo imaging of amyloid-β plaques

Abstract: A quadrupolar two-photon fluorescent probe for in vivo imaging of amyloid-β plaques is reported.

Cited by 53 publications

References 35 publications

Potential Role of Venular Amyloid in Alzheimer’s Disease Pathogenesis

Potential Role of Venular Amyloid in Alzheimer’s Disease Pathogenesis

A spiropyran-based fluorescent probe for the specific detection of β-amyloid peptide oligomers in Alzheimer's disease

Sensing Performance Investigations on Two-Photon Fluorescent Probes for Detecting β-Amyloid in Alzheimer’s Disease

Contact Info

Product

Resources

About