Chiral modulation of amyloid beta fibrillation and cytotoxicity by enantiomeric carbon dots

Ravit Malishev; Elad Arad; Susanta Kumar Bhunia; Shira Shaham-Niv; Sofiya Kolusheva; Ehud Gazit; Raz Jelinek

doi:10.1039/C8CC03235A

Chiral modulation of amyloid beta fibrillation and cytotoxicity by enantiomeric carbon dots

Ravit Malishev
, Elad Arad
, Susanta Kumar Bhunia
, Shira Shaham-Niv
, Sofiya Kolusheva
, Ehud Gazit
, Raz Jelinek^*

^*Corresponding author for this work

Ben-Gurion University of the Negev

Research output: Contribution to journal › Article › peer-review

115 Scopus citations

Abstract

Enantiomeric carbon dots (C-dots) synthesized from l-lysine or d-lysine, modulate aggregation and cytotoxicity of amyloid beta-42 (Aβ42), the primary constituent of the amyloid plaques associated with Alzheimer's disease. In particular, l-Lys-C-dots dramatically remodeled Aβ42 secondary structure and fibril morphologies, as well as inhibited Aβ42 cytotoxicity and membrane interactions.

Original language	English
Pages (from-to)	7762-7765
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	56
DOIs	https://doi.org/10.1039/C8CC03235A
State	Published - 2018

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10.1039/C8CC03235A

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abstract = "Enantiomeric carbon dots (C-dots) synthesized from l-lysine or d-lysine, modulate aggregation and cytotoxicity of amyloid beta-42 (Aβ42), the primary constituent of the amyloid plaques associated with Alzheimer's disease. In particular, l-Lys-C-dots dramatically remodeled Aβ42 secondary structure and fibril morphologies, as well as inhibited Aβ42 cytotoxicity and membrane interactions.",

author = "Ravit Malishev and Elad Arad and Bhunia, \{Susanta Kumar\} and Shira Shaham-Niv and Sofiya Kolusheva and Ehud Gazit and Raz Jelinek",

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AU - Malishev, Ravit

AU - Arad, Elad

AU - Bhunia, Susanta Kumar

AU - Shaham-Niv, Shira

AU - Kolusheva, Sofiya

AU - Gazit, Ehud

AU - Jelinek, Raz

PY - 2018

Y1 - 2018

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AB - Enantiomeric carbon dots (C-dots) synthesized from l-lysine or d-lysine, modulate aggregation and cytotoxicity of amyloid beta-42 (Aβ42), the primary constituent of the amyloid plaques associated with Alzheimer's disease. In particular, l-Lys-C-dots dramatically remodeled Aβ42 secondary structure and fibril morphologies, as well as inhibited Aβ42 cytotoxicity and membrane interactions.

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Chiral modulation of amyloid beta fibrillation and cytotoxicity by enantiomeric carbon dots

Abstract

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