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Volume 272, Number 46, Issue of November 14, 1997 pp. 28837-28840
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Gly-Pro-Arg Confers Stability Similar to Gly-Pro-Hyp in the Collagen Triple-helix of Host-Guest Peptides

(Received for publication, September 2, 1997)

Wei Yang , Virginia C. Chan , Alan Kirkpatrick ^§ , John A. M. Ramshaw ^§ and Barbara Brodsky

From the  Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854-5636 and the ^§ Commonwealth Scientific and Industrial Research Organization, Division of Molecular Science, 343 Royal Parade, Parkville, 3052, Australia

A set of host-guest peptides of the form Ac(Gly-Pro-Hyp)₃-Gly-X-Y-(Gly-Pro-Hyp)₄-Gly-Gly-NH₂ has been designed to evaluate the propensity of different Gly-X-Y triplets for the triple-helix conformation (Shah, N. K., Ramshaw, J. A. M., Kirkpatrick, A., Shah, C., and Brodsky, B. (1996) Biochemistry 35, 10262-10268). All Gly-X-Y guest triplets led to a decrease in melting temperature from the host (Gly-Pro-Hyp)₈ peptide except for Gly-Pro-Arg. In this Gly-Pro-Hyp-rich environment, Gly-Pro-Arg was found to be as stabilizing as Gly-Pro-Hyp. Decreased stability of host-guest peptides containing Gly-Pro-Lys, Gly-Pro-homo-Arg, and Gly-Arg-Hyp compared with Gly-Pro-Arg indicated a stabilization that is optimal for Arg and specific to the Y-position. Arg was found to have a similar stabilizing effect when residues other than Pro are in the X-position. Both Arg and Hyp stabilize the triple-helix preferentially in the Y-position in a stereospecific manner and occupy largely Y-positions in collagen. However, contiguous Gly-Pro-Hyp units are highly stable and promote triple-helix folding, whereas incorporation of multiple Gly-Pro-Arg triplets was destabilizing and folded slowly due to charge repulsion. In collagen, Gly-Pro-Arg may contribute maximally to local triple-helix stability while also having the potential for electrostatic interactions in fibril formation and binding.

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