| Autor: |
Kuznetsova SS; Institute of Biomedical Chemistry, Moscow, Russia., Kolesanova EF; Institute of Biomedical Chemistry, Moscow, Russia., Talanova AV; Institute of Biomedical Chemistry, Moscow, Russia; Pirogov Russian National Research Medical University, Moscow, Russia., Veselovsky AV; Institute of Biomedical Chemistry, Moscow, Russia. |
| Jazyk: |
ruština |
| Zdroj: |
Biomeditsinskaia khimiia [Biomed Khim] 2016 May; Vol. 62 (4), pp. 353-68. |
| DOI: |
10.18097/PBMC20166204353 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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