Toward the Design of Highly Efficient, Readily Accessible Peptide N-caps for the Induction of Helical Conformations

A series of novel peptide N-caps was designed with an emphasis on ease of synthesis and an abundance of hydrogen bond acceptors. Different scaffolds based on sugars, cyclic hydrocarbons, and amino acids are developed with a variety of hydrogen bond acceptors including esters, carboxyls, amides and a...

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Bibliographic Details
Published in:International journal of peptide research and therapeutics 2007-06, Vol.13 (1-2), p.237-244
Main Authors: Mimna, Richard, Tuchscherer, Gabriele, Mutter, Manfred
Format: Article
Language:English
Subjects:
Amides
Esters
Fibrillogenesis
Hydrogen bonds
Peptide synthesis
Peptides
Sulfonic acid
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Summary:A series of novel peptide N-caps was designed with an emphasis on ease of synthesis and an abundance of hydrogen bond acceptors. Different scaffolds based on sugars, cyclic hydrocarbons, and amino acids are developed with a variety of hydrogen bond acceptors including esters, carboxyls, amides and a sulfonic acid. The efficient use in solid-phase peptide synthesis was demonstrated by incorporating the N-caps to a resin-bound model peptide. Their differential helix nucleating power in aqueous buffer was determined by CD studies. Increases in peptide helicity to a significant extent are observed, leading to a discussion of N-capping efficiency versus ease of synthesis. The potential of the elaborated N-caps for the reversal of β-sheet to α-helix conformations in the context of fibrillogenesis is discussed.
ISSN:1573-3149
1573-3904
DOI:10.1007/s10989-006-9073-9