Ferrocene-assisted stabilization of collagen mimetic triple helices: solid-phase synthesis and structure |
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Authors: | Dey Subrata K Kraatz Heinz-Bernhard |
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Affiliation: | Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon, Canada. |
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Abstract: | 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. |
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