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Triple‐Helix‐Stabilizing Effects in Collagen Model Peptides Containing PPII‐Helix‐Preorganized Diproline Modules
Author(s) -
Maaßen Andreas,
Gebauer Jan M.,
Theres Abraham Elena,
Grimm Isabelle,
Neudörfl JörgMartin,
Kühne Ronald,
Neundorf Ines,
Baumann Ulrich,
Schmalz HansGünther
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201914101
Subject(s) - triple helix , collagen helix , chemistry , polyproline helix , steric effects , helix (gastropod) , stereochemistry , proline , peptide , crystallography , amino acid , biochemistry , ecology , snail , biology
Collagen model peptides (CMPs) serve as tools for understanding stability and function of the collagen triple helix and have a potential for biomedical applications. In the past, interstrand cross‐linking or conformational preconditioning of proline units through stereoelectronic effects have been utilized in the design of stabilized CMPs. To further study the effects determining collagen triple helix stability we investigated a series of CMPs containing synthetic diproline‐mimicking modules (ProMs), which were preorganized in a PPII‐helix‐type conformation by a functionalizable intrastrand C 2 bridge. Results of CD‐based denaturation studies were correlated with calculated (DFT) conformational preferences of the ProM units, revealing that the relative helix stability is mainly governed by an interplay of main‐chain preorganization, ring‐flip preference, adaptability, and steric effects. Triple helix integrity was proven by crystal structure analysis and binding to HSP47.