Investigation of pH-Dependent Collagen Triple-Helix Formation

Investigation of pH-Dependent Collagen Triple-Helix Formation

Helices on demand: Collagen peptides were engineered to form triple helices under environmental control. The replacement of the hydroxyproline (Hyp) residues in a collagen peptide with carboxylate‐modified Hyp residues gave a petide that forms a collagen triple‐helical structure at acidic pH values...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2008-01, Vol.47 (44), p.8429-8432
Hauptverfasser: Lee, Song-Gil, Lee, Jee Yeon, Chmielewski, Jean
Format: Artikel
Sprache:eng
Schlagworte:
Circular Dichroism
Collagen - chemical synthesis
Collagen - chemistry
collagen peptides
helical structures
Hydrogen-Ion Concentration
Hydroxyproline - chemistry
Models, Molecular
peptide engineering
Peptides - chemical synthesis
Peptides - chemistry
pH switches
Protein Engineering
Protein Structure, Secondary
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Beschreibung
Zusammenfassung:Helices on demand: Collagen peptides were engineered to form triple helices under environmental control. The replacement of the hydroxyproline (Hyp) residues in a collagen peptide with carboxylate‐modified Hyp residues gave a petide that forms a collagen triple‐helical structure at acidic pH values and low temperatures and adopts a monomeric, polyproline II helical conformation under neutral conditions (see scheme).
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200802224