Specific interaction between bovine cyclophilin A and synthetic analogues of cyclolinopeptide(393 views) Gallo P, Rossi F, Saviano M, Pedone C, Colonna G, Ragone R
Journal Of Biochemistry (ISSN: 0021-924x), 1998 Nov; 124(5): 880-885.
Keywords: Cyclolinopeptide A, Cyclopeptides, Cyclosporin A, Fluorimetric Binding Constants, Ppiase Inhibition Constants, Rotamase Activity, Cyclophilin A, Amino Acid Sequence, Article, Cattle, Dissociation Constant, Enzyme Activity, Enzyme Inhibition, Fluorescence, Nonhuman, Protein Interaction, Animals, Circular Dichroism, Molecular Mimicry, Peptidylprolyl Isomerase, Protein Conformation, Spectrometry, Bos Taurus, Bovinae,
Affiliations: Ctro. Stud. Biocristallografia C., Dipartimento di Chimica, Univ. Studi di Napoli Federico II, via Mezzocannone 4, 80134 Naples, Italy
Ctro. Ric. Interdipartimentale S., II Università di Napoli, via Costantinopoli 16, 80138 Naples, Italy
Dipto. di Biochimica e Biofisica, II Università di Napoli, via Costantinopoli 16, 80138 Naples, Italy
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Specific interaction between bovine cyclophilin A and synthetic analogues of cyclolinopeptide
Like cyclosporin A, cyclolinopeptide A binds specifically bovine cyclophilin A, inhibiting its peptidyl-prolyl cis-trans isomerase activity. We describe here the protein interaction with several synthetic analogues of cyclolinopeptide A, which are either homodetic or disulphide bridged heterodetic cyclopeptides characterized by different ring dimensions, in terms of dissociation and inhibition constants evaluated by fluorescence and inhibition of the enzyme activity, respectively. Dissociation constants from fluorescence experiments are practically identical and about 20-fold lower than for cyclosporin A. On the other hand, inhibition constants differ from compound to compound and are higher than for cyclosporin A. This result is therefore difficult to rationalize, but we would suggest decoupling between binding and inhibitory ability of cyclopeptides. The Pro(1) residue of cyclolinopeptide A seems to play a fundamental role in determining the inhibition of the rotamase activity of cyclophilin A, as the homodetic analogue lacking this residue does not show any inhibitory ability, Similarly, heterodetic analogues with a ring size smaller than 7 residues do not display inhibition. We presume that the sequence -Pro-Pro-Phe-Phe- and a ring size of 8 residues for homodetic cyclic peptides could be used as starting points in the targeted synthesis of cyclopeptides able to bind both cyclosporin A and calcineurin. The only peptide showing similar values of the dissociation and inhibition constant is cyclolinopeptide A. This compound can be considered a novel model for the molecular design of immunosuppressant drugs.
Specific interaction between bovine cyclophilin A and synthetic analogues of cyclolinopeptide
No results.
Specific interaction between bovine cyclophilin A and synthetic analogues of cyclolinopeptide