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Looking for a Robust, Synthetic, Fully‐Extended (2.0 5 ‐Helical) Peptide Structure – Effect of Terminal Groups
Author(s) -
Formaggio Fernando,
Crisma Marco,
Peggion Cristina,
Moretto Alessandro,
Venanzi Mariano,
Toniolo Claudio
Publication year - 2012
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.201101273
Subject(s) - chemistry , peptide , carbon atom , stereochemistry , amino acid , terminal (telecommunication) , crystallography , combinatorial chemistry , organic chemistry , ring (chemistry) , biochemistry , telecommunications , computer science
The incorporation of α‐amino acids with a quaternary α‐carbon atom into a peptide provides a tool to effectively restrict the available range of its backbone conformations. Specifically, under favorable conditions, C α,α ‐diethylglycine (Deg) homopeptides are known to preferentially adopt the fully‐extended (2.0 5 ‐helical) structure, which is characterized by the longest possible separation between two adjacent α‐amino acid C α atoms. We have investigated the influence of the nature of the N‐ and/or C‐terminal protecting (or blocking) groups on the relative stabilities of the fully‐extended conformation vs. the competing, shorter 3 10 ‐helical structure in a synthetic Deg homopeptide series.