Inhibition of trypsin by cowpea thionin: characterization, molecular modeling, and docking

• Autor(a) principal: Melo, Francislete Rodrigues
• Data de Publicação: 2002
• Outros Autores: Rigden, Daniel J., Franco, Octávio Luiz, Mello, Luciane Vieira, Ary, Maria B., Grossi- de- Sá, Maria Fátima
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UCB
• Texto Completo: http://twingo.ucb.br:8080/jspui/handle/10869/490; https://repositorio.ucb.br:9443/jspui/handle/123456789/7709
• topic: Thionin; Cowpea; Trypsin inhibitor; Molecular

Higher plants produce several families of proteins with toxic properties, which act as defense compounds against pests and pathogens. The thionin family represents one family and comprises low molecular mass cysteine-rich proteins, usually basic and distributed in different plant tissues. Here,we report the purificationandcharacterization of a new thionin from cowpea (Vigna unguiculata) with proteinase inhibitory activity. Cowpeathionininhibits trypsin, but not chymotrypsin, binding with a stoichiometry of 1:1 as shown withthe use of mass spectrometry. Previous annotations of thionins as proteinase inhibitors were based on their erroneous identification as homologues of Bowman-Birk family inhibitors. Molecular modeling experiments were used to propose a mode of docking of cowpea thionin with trypsin. Consideration of the dynamic properties of the cowpea thionin was essential to arrive at a model with favorable interface characteristics comparable with structures of trypsin-inhibitor complexes determined by X-ray crystallography. In the final model, Lys11 occupies the S1 specificity pocket of trypsin as part of a canonical style interaction.