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Inhibition of Beta-Amyloid Fibrillation by Luminescent Iridium(III) Complex Probes.

Lu L, Zhong HJ, Wang M, Ho SL, Li HW, Leung CH, Ma DL - Sci Rep (2015)

Bottom Line: We report herein the application of kinetically inert luminescent iridium(III) complexes as dual inhibitors and probes of beta-amyloid fibrillogenesis.These iridium(III) complexes inhibited Aβ1-40 peptide aggregation in vitro, and protected against Aβ-induced cytotoxicity in neuronal cells.Furthermore, the complexes differentiated between the aggregated and unaggregated forms of Aβ1-40 peptide on the basis of their emission response.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China.

ABSTRACT
We report herein the application of kinetically inert luminescent iridium(III) complexes as dual inhibitors and probes of beta-amyloid fibrillogenesis. These iridium(III) complexes inhibited Aβ1-40 peptide aggregation in vitro, and protected against Aβ-induced cytotoxicity in neuronal cells. Furthermore, the complexes differentiated between the aggregated and unaggregated forms of Aβ1-40 peptide on the basis of their emission response.

No MeSH data available.


Related in: MedlinePlus

Chemical structures of the luminescent Ir(III) complexes 1–14 which were synthesized and evaluated in this study.
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f1: Chemical structures of the luminescent Ir(III) complexes 1–14 which were synthesized and evaluated in this study.

Mentions: A library of twelve luminescent Ir(III) complexes (1–12, Fig. 1) were initially examined for their ability to interact with different forms of Aβ1–40 by emission titration. Of these twelve complexes, 12 bearing the 2-phenyl-1H-imidazo[4, 5-f][1,10]phenanthroline (phenyl-imidazo-phen) N^N ligand displayed the Ifibril/Imonomer ratio (>1.5), indicating that it possessed the highest distinguishing ability for detecting Aβ1–40 fibrils over Aβ1–40 monomers (Figure S1). However, 1–11 were unable to effectively discriminate between Aβ1–40 monomers and fibrils. Based on the structure of 12, we designed and synthesized 13 and 14. The characterization and photophysical properties of 1–14 are given in the ESI (Table S1).


Inhibition of Beta-Amyloid Fibrillation by Luminescent Iridium(III) Complex Probes.

Lu L, Zhong HJ, Wang M, Ho SL, Li HW, Leung CH, Ma DL - Sci Rep (2015)

Chemical structures of the luminescent Ir(III) complexes 1–14 which were synthesized and evaluated in this study.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4588514&req=5

f1: Chemical structures of the luminescent Ir(III) complexes 1–14 which were synthesized and evaluated in this study.
Mentions: A library of twelve luminescent Ir(III) complexes (1–12, Fig. 1) were initially examined for their ability to interact with different forms of Aβ1–40 by emission titration. Of these twelve complexes, 12 bearing the 2-phenyl-1H-imidazo[4, 5-f][1,10]phenanthroline (phenyl-imidazo-phen) N^N ligand displayed the Ifibril/Imonomer ratio (>1.5), indicating that it possessed the highest distinguishing ability for detecting Aβ1–40 fibrils over Aβ1–40 monomers (Figure S1). However, 1–11 were unable to effectively discriminate between Aβ1–40 monomers and fibrils. Based on the structure of 12, we designed and synthesized 13 and 14. The characterization and photophysical properties of 1–14 are given in the ESI (Table S1).

Bottom Line: We report herein the application of kinetically inert luminescent iridium(III) complexes as dual inhibitors and probes of beta-amyloid fibrillogenesis.These iridium(III) complexes inhibited Aβ1-40 peptide aggregation in vitro, and protected against Aβ-induced cytotoxicity in neuronal cells.Furthermore, the complexes differentiated between the aggregated and unaggregated forms of Aβ1-40 peptide on the basis of their emission response.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China.

ABSTRACT
We report herein the application of kinetically inert luminescent iridium(III) complexes as dual inhibitors and probes of beta-amyloid fibrillogenesis. These iridium(III) complexes inhibited Aβ1-40 peptide aggregation in vitro, and protected against Aβ-induced cytotoxicity in neuronal cells. Furthermore, the complexes differentiated between the aggregated and unaggregated forms of Aβ1-40 peptide on the basis of their emission response.

No MeSH data available.


Related in: MedlinePlus