Switchable proline derivatives: tuning the conformational stability of the collagen triple helix by pH changes

Christiane Siebler; Roman S Erdmann; Helma Wennemers

doi:10.1002/anie.201404935

Switchable proline derivatives: tuning the conformational stability of the collagen triple helix by pH changes

Angew Chem Int Ed Engl. 2014 Sep 22;53(39):10340-4. doi: 10.1002/anie.201404935. Epub 2014 Aug 1.

Authors

Christiane Siebler¹, Roman S Erdmann, Helma Wennemers

Affiliation

¹ Laboratorium für Organische Chemie, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich (Switzerland).

PMID: 25088036
DOI: 10.1002/anie.201404935

Abstract

(4S)-Aminoproline is introduced as a pH-sensitive probe for tuning the conformational properties of peptides and proteins. The pH-triggered flip of the ring puckering and the formation/release of a transannular H bond were used to switch the formation of collagen triple helices on and off reversibly.

Keywords: PPII helix; collagen; proline; ring pucker; stereoelectronic effects.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Circular Dichroism
Collagen / chemistry*
Hydrogen Bonding
Hydrogen-Ion Concentration
Proline / analogs & derivatives*
Protein Structure, Secondary
Protein Structure, Tertiary
Stereoisomerism

Substances

Collagen
Proline