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Inhibition of β ‐Amyloid Aggregation and Neurotoxicity by Complementary (Antisense) Peptides
Author(s) -
Heal Jonathan R.,
Roberts Gareth W.,
Christie Gary,
Miller Andrew D.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020104)3:1<86::aid-cbic86>3.0.co;2-l
Subject(s) - neurotoxicity , peptide , sequence (biology) , in vitro , amyloid (mycology) , biochemistry , dna , computational biology , chemistry , biology , toxicity , inorganic chemistry , organic chemistry
Complementary peptides are coded for by the nucleotide sequence (read 5′→3′) of the complementary strand of DNA. By reading the sequence of complementary DNA in the 3′→5′ direction, alternative complementary peptides may be derived. We describe the derivation, testing and analysis of six complementary peptides designed against β‐amyloid peptide 1‐40 (Aβ 1‐40 ). Data is presented to show that one peptide, designated 3′→5′ βCP 1‐15 , binds specifically to Aβ 1‐40 , and inhibits both fibrilisation and neurotoxicity in vitro. This suggests that complementary peptides could be useful leads for drug discovery, especially where diseases of protein misfolding are concerned.