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

Ottl J, Battistuta R, Pieper M, Tschesche H, Bode W, Kuhn K, Moroder L (1996)
FEBS LETTERS 398(1): 31-36.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
A heterotrimeric collagen peptide was designed and synthesized which contains the collagenase cleavage site (P-4-P'(9/10)) 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 (alpha 1 alpha 2 alpha 1') was found to exhibit a typical collagen-like CD spectrum at room temperature and a melting temperature (T-m) of 33 degrees 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 alpha 1' chain, Tn contrast, opposite digestion rates were measured with the catalytic Phe(79)-MMP-8 domain of HNC. Moreover, the full-length enzyme exhibits K-m values of 5 mu M and 1 mM for the heterotrimer and the single alpha 1' chain, respectively, which compare well with those reported for collagen type I (similar to 1 mu M), gelatine (similar to 10 mu M) and for octapeptides of the cleavage sequence (greater than or equal to 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.
Erscheinungsjahr
Zeitschriftentitel
FEBS LETTERS
Band
398
Ausgabe
1
Seite(n)
31-36
ISSN
PUB-ID

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Ottl J, Battistuta R, Pieper M, et al. Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases. FEBS LETTERS. 1996;398(1):31-36.
Ottl, J., Battistuta, R., Pieper, M., Tschesche, H., Bode, W., Kuhn, K., & Moroder, L. (1996). Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases. FEBS LETTERS, 398(1), 31-36. doi:10.1016/S0014-5793(96)01212-4
Ottl, J., Battistuta, R., Pieper, M., Tschesche, H., Bode, W., Kuhn, K., and Moroder, L. (1996). Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases. FEBS LETTERS 398, 31-36.
Ottl, J., et al., 1996. Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases. FEBS LETTERS, 398(1), p 31-36.
J. Ottl, et al., “Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases”, FEBS LETTERS, vol. 398, 1996, pp. 31-36.
Ottl, J., Battistuta, R., Pieper, M., Tschesche, H., Bode, W., Kuhn, K., Moroder, L.: Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases. FEBS LETTERS. 398, 31-36 (1996).
Ottl, J, Battistuta, R, Pieper, M, Tschesche, Harald, Bode, W, Kuhn, K, and Moroder, L. “Design and synthesis of heterotrimeric collagen peptides with a built-in cystine-knot - Models for collagen catabolism by matrix-metalloproteases”. FEBS LETTERS 398.1 (1996): 31-36.

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