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.
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.
Feng
Y
Y
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0343, USA.
Melacini
G
G
Taulane
J P
JP
Goodman
M
M
D055592:Biophysical Phenomena; D001703:Biophysics; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D009646:Norleucine / Q000032:analysis*; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D009904:Optical Rotation; D034444:Peptoids; D013056:Spectrophotometry, Ultraviolet
D009842:Oligopeptides; D034444:Peptoids; D009646:Norleucine; D003094:Collagen