Characterization of collagen model peptides containing 4-fluoroproline; (4(S)-fluoroproline-pro-gly)10 forms a triple helix, but (4(R)-fluoroproline-pro-gly)10 does not.
Collagen model peptide (Pro-Pro-Gly)10 has a triple helical structure and undergoes a thermal transition to a single random coil structure. The transition temperature of the analogous model peptides depends largely on amino acid substitution. Substitution of Pro by 4-hydroxyproline (Hyp) or 4-fluoroproline (fPro) has especially attracted attention because the position of substitution and chirality of the hydroxyl group or fluorine atom affect the transition temperatures. Here, we demonstrated that (4(S)-fPro-Pro-Gly)10 takes a triple helical structure, but (4(R)-fPro-Pro-Gly)10 exists in a single chain structure. This is not consistent with the case of Hyp substitution in our previous report where both (4(S)-Hyp-Pro-Gly)10 and (4(R)-Hyp-Pro-Gly)10 are in a single random coil state.
Doi
Masamitsu
M
Department of Materials Science, Wakayama National College of Technology, Gobo, Wakayama 644-0023, Japan.
Nishi
Yoshinori
Y
Uchiyama
Susumu
S
Nishiuchi
Yuji
Y
Nakazawa
Takashi
T
Ohkubo
Tadayasu
T
Kobayashi
Yuji
Y
D003094:Collagen / Q000737:chemistry*; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000031:analogs & derivatives / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism; D013816:Thermodynamics
D010455:Peptides; C431803:fluoro-proline; D003094:Collagen; D011392:Proline