The stereochemical features of 2,8,14,20-tetrakis(D-leucyl-D-valinamido)resorc[4]arenecarboxylic acid and N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide polypeptide substrate were investigated by Nuclear Magnetic Resonance spectroscopy. Proton selective relaxation parameters gave the basis of the inhibitory activity of resorcin[4]arene in the hydrolysis of polypeptide substrate by α-chymotrypsin. Results showed that an interaction between the resorcin[4]arene and α-chymotrypsin does occur, and involves the hydrophobic moiety of the macrocycle. This interaction is further reinforced by polar groups located on the side chains of the resorcin[4]arene, whereas the macrocycle/polypeptide substrate interaction is negligible. Conformational analysis and interaction studies carried out by molecular modeling are in good agreement with the NMR data, thus providing an additional support to the rationalization of the inhibitory potential of resorcin[4]arenes on α-chymotrypsin activity.

Hydrolytic inhibition of α-chymotrypsin by 2,8,14,20-tetrakis(D-leucyl-D-valinamido)resorc[4]arenecarboxylic acid: a spectroscopic NMR and computational combined approach / G., Uccello Barretta; F., Balzano; F., Aiello; L., Vanni; M., Mori; Menta, Sergio; Calcaterra, Andrea; Botta, Bruno. - In: ORGANIC & BIOMOLECULAR CHEMISTRY. - ISSN 1477-0520. - STAMPA. - 13:3(2015), pp. 916-924. [10.1039/C4OB01936a]

Hydrolytic inhibition of α-chymotrypsin by 2,8,14,20-tetrakis(D-leucyl-D-valinamido)resorc[4]arenecarboxylic acid: a spectroscopic NMR and computational combined approach

MENTA, SERGIO;CALCATERRA, ANDREA;BOTTA, Bruno
2015

Abstract

The stereochemical features of 2,8,14,20-tetrakis(D-leucyl-D-valinamido)resorc[4]arenecarboxylic acid and N-succinyl-L-alanyl-L-alanyl-L-prolyl-L-phenylalanine-4-nitroanilide polypeptide substrate were investigated by Nuclear Magnetic Resonance spectroscopy. Proton selective relaxation parameters gave the basis of the inhibitory activity of resorcin[4]arene in the hydrolysis of polypeptide substrate by α-chymotrypsin. Results showed that an interaction between the resorcin[4]arene and α-chymotrypsin does occur, and involves the hydrophobic moiety of the macrocycle. This interaction is further reinforced by polar groups located on the side chains of the resorcin[4]arene, whereas the macrocycle/polypeptide substrate interaction is negligible. Conformational analysis and interaction studies carried out by molecular modeling are in good agreement with the NMR data, thus providing an additional support to the rationalization of the inhibitory potential of resorcin[4]arenes on α-chymotrypsin activity.
2015
Resorc[4]arene derivatives
01 Pubblicazione su rivista::01a Articolo in rivista
Hydrolytic inhibition of α-chymotrypsin by 2,8,14,20-tetrakis(D-leucyl-D-valinamido)resorc[4]arenecarboxylic acid: a spectroscopic NMR and computational combined approach / G., Uccello Barretta; F., Balzano; F., Aiello; L., Vanni; M., Mori; Menta, Sergio; Calcaterra, Andrea; Botta, Bruno. - In: ORGANIC & BIOMOLECULAR CHEMISTRY. - ISSN 1477-0520. - STAMPA. - 13:3(2015), pp. 916-924. [10.1039/C4OB01936a]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/628186
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