Collagen mimics

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

Reexamination Certificate

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Details

C514S002600, C530S331000, C530S329000, C530S345000, C530S356000

Reexamination Certificate

active

07122521

ABSTRACT:
A novel collagen mimic comprising a tripeptide unit having the formula (flpYaaGly)n, where flp is 4(S)-fluoro-L-proline, is disclosed. The collagen mimic has increased stability relative to the collagen-related triple helices (ProYaaGly)n, (hypYaaGly)n, and (HypYaaGly)n.

REFERENCES:
patent: 5973112 (1999-10-01), Raines
Bella, J. et al., “Crystal and Molecular Structure of a Collagen-Like Peptide at 1.9 A Resolution,” Science (1994) 266:75-81.
Bretscher, L.E. et al., “Conformational Stability of Collagen Relies on a Stereoelectronic Effect,” J. Am. Chem. Soc. (2001) 123:777-778.
Eberhardt, E.S. et al., “Inductive Effects on the Energetics of Prolyl Peptide Bond Isomerization: Implications for Collagen Foling and Stability,” Journal of the American Chemical Society, (1996) 118:12261-12266.
Gottieb, A.A., et al., “Incorporation of cis- and trans-4-Fluoro-L-prolines into Proteins and Hydroxylation of the trans Isomer During Collagen Biosynthesis,” Biochemistry (1965) 4:2507-2513.
Hodges, J.A. et al., “The Effect of Fluoroproline in the X-Position of the Stability of the Collagen Triple Helix,” Abstract, Americal Peptide Symposium Jul. 23, 2003.
Holmgren, S.K. et al., “Code for collagen's stability deciphered,” Nature (1998) 392:666-667.
Panasik, N., Jr. et al., “Inductive effects on the structure of proline residues,” Int. J. Peptide Protein Res. (1994) 44:262-269.
Sakakibara, S., et al., “Synthesis of (Pro-Hyp-Gly)n of defined molecular weights Evidence for the stabilization of collagen triple helix by hydroxypyroline,” (1973) 303:198-202, Biochimica ef Biophysica Acta (1973) vol. 303 pp. 198-202.

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