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Modeling enzyme–inhibitor interactions in serine proteases

✍ Scribed by Maria João Ramos; André Melo; Elsa S. Henriques; José A. N. F. Gomes; Nathalie Reuter; Bernard Maigret; Wely B. Floriano; Marco A. C. Nascimento

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
309 KB
Volume
74
Category
Article
ISSN
0020-7608

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✦ Synopsis

We are interested in modeling enzyme᎐inhibitor interactions with a view to improve the understanding of the biology of these processes. The present work focuses, therefore, on the research on enzyme᎐inhibitor interactions using two highly homologous enzymes as our models: ␤-factor XIIa and trypsin. This study so far has Ž . focused on the following: 1 arginine᎐carboxylate interactions such as the one occurring in the ''binding pocket'' of ␤-factor XIIa with an inhibitor; according to the present calculations, the neutral form is usually more stable than is the zwitterion in hydrophobic Ž . environments as in the case of the above-mentioned complex. 2 Interactions present in the contact region between trypsin and PTI; the contribution of some amino acids of that region to the binding energy of the complex trypsin᎐PTI was determined using free-Ž . energy simulation methods. 3 Interactions involved in the inhibition of trypsin by PTI; Ž . hybrid quantum-classical mechanical calculations LSCF were performed to further this point.

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