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 deg 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.
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