Elucidating pH-dependent collagen triple helix formation through interstrand hydroxyproline-glutamic acid interactions.
Chembiochem : a European journal of chemical biology
confidence
Key findings
Describes pH-dependent interstrand hydroxyproline-glutamic acid interactions affecting triple-helical stability of collagen peptides; no clinical/biological endpoints.
View source on PubMed (PMID 25530443) ↗
- Sample size
- Not reported
- Population
- In vitro collagen-mimetic peptides (research study)
- Dosing
- Not reported
- Duration
- Not reported
- Route
- Not reported
- Blinding
- not_reported
- Controls
- not_reported
- Drug class
- peptide
Full abstract
Here, we describe systematic explorations into the molecular basis underlying hydroxyproline-mediated interstrand interactions on the triple-helical stability of collagen-mimetic peptides containing glutamic acid residues. Our studies reveal that the triple-helical stability of these peptides relies on the existence of interstrand interactions between hydroxyprolines and glutamic acid residues that are pH dependent. These unique interactions have been used to engineer collagen peptides that form triple helices on demand through pH control.