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Recipe for β‐Sheets: Foldamers Containing Amyloidogenic Peptide Sequences
Author(s) -
Spencer Ryan,
Chen Kevin H.,
Manuel Gerald,
Nowick James S.
Publication year - 2013
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201300221
Subject(s) - pentapeptide repeat , chemistry , peptide , peptidomimetic , solid phase synthesis , sequence (biology) , peptide synthesis , peptide sequence , amino acid , foldamer , beta sheet , stereochemistry , combinatorial chemistry , biochemistry , gene
Abstract This paper describes a new class of macrocyclic peptides that fold to form β‐sheet structures. These macrocyclic β‐sheets consist of a peptide sequence strand linked through two δ‐linked ornithine turn units to a peptide template strand containing a single N ‐methyl amino acid. The macrocycles were readily prepared from commercially available amino acids by solid‐phase peptide synthesis followed by solution‐phase cyclization. 1 H NMR spectroscopic studies showed that macrocycles containing amyloidgenic pentapeptide sequences from amyloid β‐peptide, tau protein, the B‐chain of insulin, and human prion protein fold to form β‐sheet structures.