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Towards Foldameric Miniproteins: A Helix‐Turn‐Helix Motif
Author(s) -
Ożga Katarzyna,
DrewniakŚwitalska Magda,
RudzińskaSzostak Ewa,
Berlicki Łukasz
Publication year - 2021
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.202100090
Subject(s) - helix (gastropod) , helix turn helix , circular dichroism , protein secondary structure , turn (biochemistry) , chemistry , folding (dsp implementation) , nuclear magnetic resonance spectroscopy , crystallography , structural motif , peptide , stereochemistry , sequence (biology) , protein folding , alpha helix , peptide sequence , triple helix , biochemistry , biology , electrical engineering , engineering , ecology , repressor , snail , gene , transcription factor
Numerous beta‐amino acid containing peptides forming secondary structures have been already described, however the design of higher‐order structures remains poorly explored. The methodology allowing construction of sequence patterns containing few rigid secondary element was proposed and experimentally validated. On the basis of 9/10/9/12‐helix containing cis ‐2‐aminocyclopentanecarboxylic acid (cis‐ACPC) residues arranged in an ααββ sequence pattern, a conformationally stable helix‐turn‐helix structure was designed. The connection between two helices was also constructed using cis‐ACPC residues. Five examples of designed peptides were obtained and analyzed using circular dichroism and nuclear magnetic resonance spectroscopy, which confirmed the assumed way of folding. The NMR structure was calculated for the peptide with the highest number of non‐sequential contacts.