Transglutaminase surface recognition by peptidocalix[4]arene diversomers

Simona, Francese; Anna, Cozzolino; Caputo, Ivana; Esposito, Carla; Martino, Marco; Gaeta, Carmine; Troisi, Francesco; Neri, Placido

doi:10.1016/J.TETLET.2005.01.078

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A series of N-linked tetrakis(tetrapeptido)calix[4]arene diversomers, 3A–P, has been synthesized by coupling of a cone calix[4]arene tetracarboxylic acid chloride with tetrapeptides 1A–P obtained in a parallel fashion. The inhibition activity of 3A–P towards tissue and microbial transglutaminase was evaluated by in vitro assays with a labeled substrate. Kinetic analysis using one of the most active derivatives (3A) showed a noncompetitive inhibition with respect to the amino acceptor substrate and an uncompetitive inhibition with respect to amino donor substrate. Experimental results are in accordance with an inhibition due to a protein specific surface recognition on a region noncomprising the enzyme active site.

Titolo:	Transglutaminase surface recognition by peptidocalix[4]arene diversomers
Autori:	SIMONA FRANCESE ANNA COZZOLINO CAPUTO, Ivana ESPOSITO, Carla MARTINO, Marco GAETA, Carmine TROISI, FRANCESCO NERI, Placido mostra contributor esterni nascondi contributor esterni
Data di pubblicazione:	2005
Rivista:	TETRAHEDRON LETTERS
Abstract:	A series of N-linked tetrakis(tetrapeptido)calix[4]arene diversomers, 3A–P, has been synthesized by coupling of a cone calix[4]arene tetracarboxylic acid chloride with tetrapeptides 1A–P obtained in a parallel fashion. The inhibition activity of 3A–P towards tissue and microbial transglutaminase was evaluated by in vitro assays with a labeled substrate. Kinetic analysis using one of the most active derivatives (3A) showed a noncompetitive inhibition with respect to the amino acceptor substrate and an uncompetitive inhibition with respect to amino donor substrate. Experimental results are in accordance with an inhibition due to a protein specific surface recognition on a region noncomprising the enzyme active site.
Handle:	http://hdl.handle.net/11386/1058698
Appare nelle tipologie:	1.1.2 Articolo su rivista con ISSN

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