Unknown

Dataset Information

0

Synthesis and Characterization of Thiophene-based Donor-Acceptor-Donor Heptameric Ligands for Spectral Assignment of Polymorphic Amyloid-? Deposits.


ABSTRACT: Protein deposits are associated with many devastating diseases and fluorescent ligands able to visualize these pathological entities are essential. Here, we report the synthesis of thiophene-based donor-acceptor-donor heptameric ligands that can be utilized for spectral assignment of distinct amyloid-? (A?) aggregates, one of the pathological hallmarks in Alzheimer's disease. The ability of the ligands to selectively distinguish A? deposits was abolished when the chemical composition of the ligands was altered. Our findings provide the structural and functional basis for the development of new fluorescent ligands that can distinguish between aggregated proteinaceous species consisting of the same peptide or protein. In addition, such ligands might aid in interpreting the potential role of polymorphic A? deposits in the pathogenesis of Alzheimer's disease.

SUBMITTER: Lantz L 

PROVIDER: S-EPMC7318160 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Synthesis and Characterization of Thiophene-based Donor-Acceptor-Donor Heptameric Ligands for Spectral Assignment of Polymorphic Amyloid-β Deposits.

Lantz Linda L   Shirani Hamid H   Klingstedt Therése T   Nilsson K Peter R KPR  

Chemistry (Weinheim an der Bergstrasse, Germany) 20200515 33


Protein deposits are associated with many devastating diseases and fluorescent ligands able to visualize these pathological entities are essential. Here, we report the synthesis of thiophene-based donor-acceptor-donor heptameric ligands that can be utilized for spectral assignment of distinct amyloid-β (Aβ) aggregates, one of the pathological hallmarks in Alzheimer's disease. The ability of the ligands to selectively distinguish Aβ deposits was abolished when the chemical composition of the liga  ...[more]

Similar Datasets

| S-EPMC4601348 | biostudies-literature
| S-EPMC7898931 | biostudies-literature
| S-EPMC4221846 | biostudies-literature
| S-EPMC10995944 | biostudies-literature
| S-EPMC4517144 | biostudies-literature
| S-EPMC6415233 | biostudies-literature
| S-EPMC4557812 | biostudies-literature
| S-EPMC3132408 | biostudies-literature
| S-EPMC6432059 | biostudies-literature
| S-EPMC3884759 | biostudies-literature