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J Biol Chem, Vol. 275, Issue 19, 14532-14536, May 12, 2000

The Collagen-like Peptide (GER)₁₅GPCCG Forms pH-dependent Covalently Linked Triple Helical Trimers^*

Diane E. Mechling and Hans Peter Bächinger^§¶

From the  Shriners Hospital for Children and ^§ Department of Biochemistry and Molecular Biology, Oregon Health Sciences University, Portland, Oregon 97201

A collagen-like peptide with the sequence (GER)₁₅ GPCCG was synthesized to study the formation of a triple helix in the absence of proline residues. This peptide can form a triple helix at acidic and basic pH, but is insoluble around neutral pH. The formation of a triple helix can be used to covalently oxidize the cysteine residues into a disulfide knot. Three disulfide bonds are formed between the three chains as has been found at the carboxyl-terminal end of the type III collagen triple helix. This is a new method to covalently link collagen-like peptides with a stereochemistry that occurs in nature. The peptide undergoes a reversible, cooperative triple helix  coil transition with a transition midpoint (T_m) of 17 to 20 °C at acidic pH and 32 to 37 °C at basic pH. At acidic pH there was little influence of the T_m on the salt concentration of the buffer. At basic pH increasing the salt concentration reduced the T_m to values comparable to the stability at acidic pH. These experiments show that the tripeptide unit GER which occurs frequently in collagen sequences can form a triple helical structure in the absence of more typical collagen-like tripeptide units and that charge-charge interactions play a role in the stabilization of the triple helix of this peptide.

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