Like cyclosporin A, cyclolinopeptide A binds specifically bovine cyclophilin A, inhibiting its peptidyl-prolyl cis-trans isomerase activity. We describe the protein interaction with several synthetic analogues of cyclolinopeptide A in terms of dissociation and inhibition constants evaluated by fluorescence and inhibition of the enzyme activity.

Specific interaction between cyclophylin A and synthetic analogues of cyclolinopeptide A / Gallo, P.; Rossi, Filomena; Saviano, M.; Pedone, C.; Colonna, G.; Ragone, R.. - In: JOURNAL OF BIOCHEMISTRY. - ISSN 0021-924X. - STAMPA. - 124:(1998), pp. 880-885.

Specific interaction between cyclophylin A and synthetic analogues of cyclolinopeptide A

ROSSI, FILOMENA;
1998

Abstract

Like cyclosporin A, cyclolinopeptide A binds specifically bovine cyclophilin A, inhibiting its peptidyl-prolyl cis-trans isomerase activity. We describe the protein interaction with several synthetic analogues of cyclolinopeptide A in terms of dissociation and inhibition constants evaluated by fluorescence and inhibition of the enzyme activity.
1998
Specific interaction between cyclophylin A and synthetic analogues of cyclolinopeptide A / Gallo, P.; Rossi, Filomena; Saviano, M.; Pedone, C.; Colonna, G.; Ragone, R.. - In: JOURNAL OF BIOCHEMISTRY. - ISSN 0021-924X. - STAMPA. - 124:(1998), pp. 880-885.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/458884
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