Journal article
Alkylation of γ-Azaproline Creates Conformationally Adaptable Proline Derivatives for pH-Responsive Collagen Triple Helices.
- Aronoff MR Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, 8093, Zürich, Switzerland.
- Egli J Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, 8093, Zürich, Switzerland.
- Schmitt A Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, 8093, Zürich, Switzerland.
- Wennemers H Laboratory of Organic Chemistry, ETH Zürich, Vladimir-Prelog-Weg 3, 8093, Zürich, Switzerland.
- 2020-02-12
Published in:
- Chemistry (Weinheim an der Bergstrasse, Germany). - 2020
collagen
conformation
pH response
peptides
proline
Alkylation
Aza Compounds
Collagen
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Peptides
Proline
English
Cγ -substituted proline derivatives are valuable tools for developing functionalized collagen peptides for biological and materials investigations, yet the stereochemistry at Cγ can produce undesired steric or stereoelectronic constraints. Alkylated γ-azaproline (γ-azPro) derivatives are proline mimetics that lack a stereogenic center at the γ-position of the ring and can thus utilize the invertibility of nitrogen to adapt their conformation. NMR spectroscopic analyses and DFT calculations highlighted how alkylated γ-azPro derivatives are conformationally dynamic and adopt conformational preferences through ring pucker flip along with nitrogen inversion. Lastly, incorporation of alkylated γ-azPro into collagen peptides produced functionalized pH-responsive triple helices with similar thermal stabilities, regardless of their placement in the Xaa or Yaa position within the characteristic Xaa-Yaa-Gly repeating unit of collagen peptides.
- Language
-
- English
- Open access status
- closed
- Identifiers
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- DOI 10.1002/chem.201905768
- PMID 32043659
- Persistent URL
- https://sonar.ch/global/documents/185491
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