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Frontispiece: Isolated Collagen Mimetic Peptide Assemblies Have Stable Triple‐Helix Structures
Author(s) -
Lalande Mathieu,
CombyZerbino Clothilde,
Bouakil Mathilde,
Dugourd Philippe,
Chirot Fabien,
Poully JeanChristophe
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201885265
Subject(s) - triple helix , collagen helix , hydroxylation , chemistry , helix (gastropod) , peptide , proline , tandem , stereochemistry , biophysics , materials science , biochemistry , amino acid , biology , enzyme , ecology , snail , composite material
The stability of the remarkable triple helix structure of collagen, the most abundant protein in mammalian organisms, has been investigated by tandem‐ion mobility and mass spectrometry. It was shown that collagen mimetic peptides can retain robust triple helix configurations in the absence of solvent. Moreover, the enhancement of the structural stability of the triple helix motifs through proline hydroxylation, known from solution‐phase measurements, is preserved in the gas phase. This provides new arguments to support that the origin of this stabilization is partially intrinsic, possibly involving stereoelectronic effects. For more details, see the Communication by J.‐C. Poully et al. on page 13728 ff.