Inviting C5-Trifluoromethylated Pseudoprolines into Collagen Mimetic Peptides - Structure et Dynamique des Biomolécules
Article Dans Une Revue Biomacromolecules Année : 2023

Inviting C5-Trifluoromethylated Pseudoprolines into Collagen Mimetic Peptides

Résumé

Numerous collagen mimetic peptides (CMPs) have been engineered using proline derivatives substituted at their C(3) and/or C(4) position in order to stabilize or functionalize collagen triple-helix mimics. However, no example has been reported so far with C(5) substitutions. Here, we introduce a fluorinated CMP incorporating trifluoromethyl groups at the C(5) position of pseudoproline residues. In tripeptide models, our CD, NMR, and molecular dynamics (MD) studies have shown that, when properly arranged, these residues meet the structural requirements for a triple-helix assembly. Two host–guest CMPs were synthesized and analyzed by CD spectroscopy. The NMR analysis in solution of the most stable confirmed the presence of structured homotrimers that we interpret as triple helices. MD calculations showed that the triple-helix model remained stable throughout the simulation with all six trifluoromethyl groups pointing outward from the triple helix. Pseudoprolines substituted at the C(5) positions appeared as valuable tools for the design of new fluorinated collagen mimetic peptides.
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hal-04265852 , version 1 (31-10-2023)

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Anaïs Terrien, Keyvan Rahgoshay, Emelyne Renaglia, Nathalie Lensen, Yves Jacquot, et al.. Inviting C5-Trifluoromethylated Pseudoprolines into Collagen Mimetic Peptides. Biomacromolecules, 2023, 24 (4), pp.1555-1562. ⟨10.1021/acs.biomac.2c01242⟩. ⟨hal-04265852⟩
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