[논문]Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot Models for collagen catabolism by matrix-metalloproteases

Ottl, Johannes; Battistuta, Roberto; Pieper, Michael; Tschesche, Harald; Bode, Wolfram; Kü; hn, Klaus; Moroder, Luis

doi:10.1016/S0014-5793(96)01212-4

[해외논문] Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot Models for collagen catabolism by matrix-metalloproteases 원문보기

FEBS letters, v.398 no.1, 1996년, pp.31 - 36

Ottl, Johannes (Max-Planck-Institut fü) , Battistuta, Roberto (r Biochemie, AG Bioorganische Chemie, Am Klopferspitz 18A, 82152 Martinsried, Germany) , Pieper, Michael (Max-Planck-Institut fü) , Tschesche, Harald (r Biochemie, AG Bioorganische Chemie, Am Klopferspitz 18A, 82152 Martinsried, Germany) , Bode, Wolfram (Universitä) , Kühn, Klaus (t Bielefeld, Fakultä) , Moroder, Luis (t Chemie und Biochemie I, Bielefeld, Germany)

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AbstractA heterotrimeric collagen peptide was designed and synthesized which contains the collagenase cleavage site (P4-P′910) of type I collagen linked to a C-terminal cystine-knot, and N-terminally extended with (Gly-Pro-Hyp)5 triplets for stabilization of the triple-helical conformation. By employing a newly developed regioselective cysteine pairing strategy based exclusively on thiol disulfide exchange reactions, we succeeded in assembling in high yields and in a reproducible manner the triple-stranded cystine peptide. While the single chains showed no tendency to self-association into triple helices, the heterotrimer (α1α2α1′) was found to exhibit a typical collagen-like CD spectrum at room temperature and a melting temperature (Tm) of 33°C. This triple-helical collagen-like peptide is cleaved by the full-length human neutrophil collagenase (MMP-8) at a single locus fully confirming the correct raster of the heterotrimer. Its digestion proceeds at rates markedly higher than that of a single α1′ chain. In contrast, opposite digestion rates were measured with the catalytic Phe79-MMP-8 domain of HNC. Moreover, the full-length enzyme exhibits Km values of 5 μM and 1 mM for the heterotrimer and the single α1′ chain, respectively, which compare well with those reported for collagen type I (∼ 1 μM), gelatine (∼ 10 μM) and for octapeptides of the cleavage sequence (≥1 mM). The high affinity of the MMP-8 for the triple-helical heterotrimer and the fast digestion of this collagenous peptide confirm the decisive role of the hemopexin domain in recognition and possibly, partial unfolding of collagen.

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