Triple helical stabilities of guest-host collagen mimetic structures.
The peptoid Nleu (N-isobutylglycine) has been successfully incorporated into a series of collagen mimetics composed of Gly-Pro-Nleu and Gly-Nleu-Pro sequences and has been able to maintain triple helices in appropriate structures. The achiral trimeric sequence Gly-Nleu-Nleu as a guest sequence in structures such as Ac-(Gly-Pro-Hyp)3-(Gly-Nleu-Nleu)3-(Gly-Pro-Hyp)3-NH2 retains triple helicity. As an extension of this study, we report, in this paper, on a series of guest-host collagen mimetic structures in which Gly-Nleu-Pro sequences are employed as the host. The guest sequences for these guest-host structures include Gly-Nleu-Nleu and Gly-Nx-Pro sequences where Nx is composed of a variety of alkyl and aralkyl peptoid residues. From these guest-host collagen mimetic structures, we are able to elucidate the contributions of hydrophobic and steric effects on triple helix formation. The Gly-Nleu-Pro sequences have been shown to be effective in inducing triple helicity. Conformational characterization of the guest-host collagen mimetic structures was established by techniques such as temperature-dependent optical rotation measurements and circular dichroism (CD) spectroscopy.
Kwak
J
J
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0343, USA.
Jefferson
E A
EA
Bhumralkar
M
M
Goodman
M
M
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D003094:Collagen / Q000737:chemistry*; D005998:Glycine / Q000031:analogs & derivatives / Q000737:chemistry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009904:Optical Rotation; D010455:Peptides / Q000737:chemistry*; D034444:Peptoids; D011487:Protein Conformation; D011489:Protein Denaturation; D017433:Protein Structure, Secondary; D013696:Temperature
C119042:N-isobutylglycine; D010455:Peptides; D034444:Peptoids; D003094:Collagen; D005998:Glycine