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Amyloid Inhibitors: Lysine‐Derived Carbon Dots for Chiral Inhibition of Prion Peptide Fibril Assembly (Adv. Therap. 4/2018)
Author(s) -
Arad Elad,
Bhunia Susanta Kumar,
Jopp Jürgen,
Kolusheva Sofiya,
Rapaport Hanna,
Jelinek Raz
Publication year - 2018
Publication title -
advanced therapeutics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.125
0ISSN - 2366-3987
DOI - 10.1002/adtp.201870008
Subject(s) - enantiomer , lysine , peptide , chemistry , asymmetric carbon , fibril , amyloid fibril , amyloid (mycology) , stereochemistry , biophysics , biochemistry , amyloid β , amino acid , optically active , biology , organic chemistry , medicine , inorganic chemistry , disease , pathology
In article number 1800006 , Raz Jelinek and co‐workers report that enantiomeric C‐dots, synthesized from either d ‐Lysine or l ‐Lysine, interfere with aggregation of the amyloidogenic determinant of the prion protein. The interactions of the chiral Lys‐C‐dots with the amyloidogenic determinant, as well as with membrane bilayers, appear to be stereoselective, with the l ‐Lys‐C‐dots inhibiting amyloidogenic aggregation more effectively than d ‐Lys‐C‐dots.