Recipe for β‐Sheets: Foldamers Containing Amyloidogenic Peptide Sequences. Issue 17 (15th May 2013)

• Record Type: Journal Article
• Authors: Spencer, Ryan; Chen, Kevin H.; Manuel, Gerald; Nowick, James S.
• Other Names: Tomasini Claudia sponsoringEditor.; Juc Ivan sponsoringEditor.; Aitken David J. sponsoringEditor.; Fülöp Ferenc sponsoringEditor.
• Is Part Of: European journal of organic chemistry. Issue 17(2013)
• Page Start: 3523
• Page End: 3528
• Publication Date: 2013-05-15
• Subjects: Foldamers -- Peptides -- Amino acids -- Macrocycles; Chemistry, Organic -- Periodicals; Organic compounds -- Synthesis -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1002/ejoc.201300221
• Languages: English
• ISSNs: 1434-193X

Abstract

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. Abstract : Recipe for β‐Sheets: Combine one N ‐methyl‐amino acid, two δ‐linked ornithine turn units, and nine α‐amino acids by solid‐phase peptide synthesis. Cyclize in solution, deprotect, and purify by RP‐HPLC. Confirm folding by 1 H NMR ROESY and magnetic anisotropy studies. Serve to laboratories interested in studying and inhibiting amyloid aggregation or studying β‐sheet assembly.