Curcacycline B, a cyclic nonapeptide from Jatropha curcas enhancing rotamase activity of cyclophilin

Tetrahedron Letters

Volumn 38, Issue 16, 1997, Pages 2845-2848

  Auvin, Catherine ^a   Baraguey, Carine ^a   Blond, Alain ^a   Lezenven, Françoise ^a   Pousset, Jean Louis ^a   Bodo, Bernard ^a  

^a MUSÉUM NATIONAL D'HISTOIRE NATURELLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPEPTIDE; CYCLOPHILIN; CYCLOPHILIN B; NONAPEPTIDE;

ARTICLE; DRUG DEGRADATION; DRUG ISOLATION; DRUG STRUCTURE; MASS SPECTROMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHYTOCHEMISTRY;

EID: 0030987770     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4039(97)00495-4     Document Type: Article

References (14)

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9. (c) van den Berg, A.J.J.; Horsten, S.F.A.J.; Kettenes-van den Bosch, J.J.; Beukelman, C.J.; Kroes, B.H.; Leeflang, B.R.; Labadie, R.P. Phytochemistry, 1996, 42, 129-133.
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11. 8-).
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13. The PPIase activity was assessed with the a-chymotrypsin-coupled enzymatic assay. The substrate was the tetrapeptide Suc-Ala-Ala-Pro-Phe-pNA which is in an equilibrum between cis (∼10%) and trans (∼90%) forms in aqueous solution. The C-terminal blocking group (pNA) of the peptide substrate is cleaved instantaneously by α-chymotrypsin only if the Ala-Pro bond is in the trans form. The cis peptide spontaneously converts at a slow rate to the trans isomer which is cleaved by α-chymotrypsin. Release of the chromogenic group (p-nitroaniline) is monitored by measuring the absorbance at λ=410 nm as a function of time. In the presence of a PPIase the rate of cis/trans isomerization of peptides is accelerated, which in turn shortens the life time of the blocked peptide.
14. In a plastic cuvette were added 2 ml of ice cold assay buffer (40 mM Na-HEPES, 1 mM EDTA, 5 mM DTT, 150 mM NaCl, 0.015% Triton X-100, pH 7.9) 10 μL human cyclophilin-B (89 μM), 25 μL of peptide substrate (4.8 mg / 2 mL DMSO) and 6 μL of 1 at various concentration in MeOH. The reaction was initiated by addition of 20 μL of α-chymotrypsin (20 mg/mL in 1 mM HCl). The absorbance at 410 nm versus time was monitored for 180 s using an UVIKON 930 spectrophotometer.