title: Elucidating pH-dependent collagen triple helix formation through interstrand hydroxyproline-glutamic acid interactions.
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.
authors.affiliation: Institute of Bioengineering and Nanotechnology, 31 Biopolis Way, The Nanos, Singapore 138669 (Singapore).
authors.forename: Liwei
authors.initials: L
authors.lastname: Chen
authors.forename: Shuting
authors.initials: S
authors.lastname: Cai
authors.forename: Jaehong
authors.initials: J
authors.lastname: Lim
authors.forename: Su Seong
authors.initials: SS
authors.lastname: Lee
authors.forename: Song-Gil
authors.initials: SG
authors.lastname: Lee
mesh_terms: D003094:Collagen / Q000737:chemistry*; D018698:Glutamic Acid / Q000737:chemistry*; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D006909:Hydroxyproline / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation
chemical_list: D010455:Peptides; D018698:Glutamic Acid; D003094:Collagen; D006909:Hydroxyproline
keywords: collagen; hydrogen bonding; hydroxyproline; pH switches; peptides