Collagen-based structures containing the peptoid residue N-isobutylglycine (Nleu): Synthesis and biophysical studies of Gly-Pro-Nleu sequences by circular dichroism, ultraviolet absorbance, and optical rotation
Corresponding Author
Yangbo Feng
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343Search for more papers by this authorGiuseppe Melacini
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Search for more papers by this authorJoseph P. Taulane
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Search for more papers by this authorMurray Goodman
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Search for more papers by this authorCorresponding Author
Yangbo Feng
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343Search for more papers by this authorGiuseppe Melacini
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Search for more papers by this authorJoseph P. Taulane
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Search for more papers by this authorMurray Goodman
Department of Chemistry and Biochemistry, University of California, San Diego La Jolla, California 92093-0343
Search for more papers by this authorAbstract
A peptoid residue N-isobutylglycine (Nleu) was introduced as a proline surrogate in collagen-like triple helical structures. A series of single chain and template-assembled collagen-based peptide-peptoid structures composed of Gly-Pro-Nleu sequences were prepared by solid-phase segment condensation methods. Both a synthetic route in solution and a solid phase method were employed to couple the KTA (cis,cis-1,3,5-trimethylcyclohexane-1,3,5-tricarboxylic acid, also known as the Kemp triacid) based template, KTA-(Gly-OH)3, to peptide-peptoid chains. Biophysical studies using CD, uv absorbance, and optical rotation measurements demonstrated that these compounds form triple-helical structures when the chains are longer than critical lengths. Results from melting curve measurements indicated that the Gly-Pro-Nleu sequence is comparable to the Gly-Pro-Pro sequence in stabilizing a triple-helical conformation. The KTA-based template stabilized triple-helical structures as can be seen by the increased melting temperatures as compared to equivalent single chain molecules. In addition, the template reduced the minimum chain length necessary to form a triple helix from six to only three trimer repeats. © 1996 John Wiley & Sons, Inc.
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