Ferrocene-assisted stabilization of collagen mimetic triple helices: solid-phase synthesis and structure.
A series of ferrocene-containing collagen models Fc-CO-(Pro-Hyp-Gly)n-Cys (n = 4 (1), 6 (2), 7 (3), 8 (4), 9 (5)) were synthesized by solid-phase synthesis. Biophysical studies using circular dichroism (CD) show that these collagen analogues form triple-helical conformations, and the peptides showed a range of thermal stabilities ((T(m)), 38-74 degrees C). Results also indicate that the ferrocene (Fc)-labeled collagen models possesses a higher triple-helical propensity than the unlabeled collagen models as demonstrated by the higher melting temperatures and thermodynamic parameters, and we conclude that the Fc group at the N-terminal position of the peptide strands increases the stability of the triple helix.
Dey
Subrata K
SK
Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Canada.
Kraatz
Heinz-Bernhard
HB
D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D005296:Ferrous Compounds / Q000737:chemistry*; D000075163:Metallocenes; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
D005296:Ferrous Compounds; D000075163:Metallocenes; D010455:Peptides; D003094:Collagen; C004998:ferrocene