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Published online before print March 9, 2004, 10.1110/ps.03501704
Protein Science (2004), 13:893-902. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Equilibrium thermal transitions of collagen model peptides

Anton V. Persikov, Yujia Xu1 and Barbara Brodsky

University of Medicine and Dentistry of New Jersey (UMDNJ)–Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA

(RECEIVED October 30, 2003; FINAL REVISION December 31, 2003; ACCEPTED January 7, 2004)



Abstract

The folding of collagen in vitro is very slow and presents difficulties in reaching equilibrium, a feature that may have implications for in vivo collagen function. Peptides serve as good model systems for examining equilibrium thermal transitions in the collagen triple helix. Investigations were carried out to ascertain whether a range of synthetic triple-helical peptides of varying sequences can reach equilibrium, and whether the triple helix to unfolded monomer transition approximates a two-state model. The thermal transitions for all peptides studied are fully reversible given sufficient time. Isothermal experiments were carried out to obtain relaxation times at different temperatures. The slowest relaxation times, on the order of 10–15 h, were observed at the beginning of transitions, and were shown to result from self-association limited by the low concentration of free monomers, rather than cis–trans isomerization. Although the fit of the CD equilibrium transition curves and the concentration dependence of Tm values support a two-state model, the more rigorous comparison of the calorimetric enthalpy to the van’t Hoff enthalpy indicates the two-state approximation is not ideal. Previous reports of melting curves of triple-helical host–guest peptides are shown to be a two-state kinetic transition, rather than an equilibrium transition.

Keywords: collagen; triple helix; peptide; equilibrium; thermodynamics; two-state model; relaxation

Abbreviations: The standard single-letter and three-letter codes have been used to denote common amino acids • 4R-hydroxyproline is denoted by O (single-letter code) and Hyp (three-letter code). CD, circular dichroism • Tm, melting temperature, determined at F = f1/2 of transition curves • Tmeq, melting temperature in transitions shown to be at equilibrium • {Delta}Hcal, calorimetric enthalpy • {Delta}HvH, van’t Hoff enthalpy

Reprint requests to: Barbara Brodsky, UMDNJ–Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA; e-mail: brodsky{at}umdnj.edu; fax: (732) 235-4783.

1 Present address: Department of Chemistry, Hunter College, 695 Park Avenue, New York, NY 10021, USA.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03501704.


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