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Biomed Khim ; 62(4): 353-68, 2016 May.
Artigo em Russo | MEDLINE | ID: mdl-27562989

RESUMO

Plant seed knottins, mainly from the Cucurbitacea family, and sunflower seed trypsin inhibitor (SFTI 1) are the most low-molecular canonical peptide inhibitors of serine proteases. High efficiency of inhibition of various serine proteases, structure rigidity together with the possibility of limited variations of amino acid sequences, high chemical stability, lack of toxic properties, opportunity of production by either chemical synthesis or use of heterologous expression systems make these inhibitors attractive templates for design of new compounds for regulation of therapeutically significant serine protease activities. Hence the design of such compounds represents a prospective research field. The review considers structural characteristics of these inhibitors, their properties, methods of preparation and design of new analogs. Examples of successful employment of natural serine protease inhibitors belonging to knottin family and SFTI 1 as templates for the design of highly specific inhibitors of certain proteases are given.


Assuntos
Miniproteínas Nó de Cistina/química , Peptídeos Cíclicos/farmacologia , Proteínas de Plantas/química , Inibidores de Serina Proteinase/farmacologia , Animais , Miniproteínas Nó de Cistina/metabolismo , Descoberta de Drogas , Humanos , Peptídeos Cíclicos/síntese química , Peptídeos Cíclicos/química , Proteínas de Plantas/metabolismo , Ligação Proteica , Inibidores de Serina Proteinase/síntese química , Inibidores de Serina Proteinase/química
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