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Recombinant Cathepsin L of Tribolium castaneum and Its Potential in the Hydrolysis of Immunogenic Gliadin Peptides.
Dvoryakova, Elena A; Klimova, Maria A; Simonyan, Tatiana R; Dombrovsky, Ivan A; Serebryakova, Marina V; Tereshchenkova, Valeriia F; Dunaevsky, Yakov E; Belozersky, Mikhail A; Filippova, Irina Y; Elpidina, Elena N.
Afiliación
  • Dvoryakova EA; A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Klimova MA; Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Simonyan TR; Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Dombrovsky IA; Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Serebryakova MV; A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Tereshchenkova VF; Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Dunaevsky YE; A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Belozersky MA; A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Filippova IY; Department of Chemistry, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Elpidina EN; A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119991 Moscow, Russia.
Int J Mol Sci ; 23(13)2022 Jun 23.
Article en En | MEDLINE | ID: mdl-35806001
Wheat gliadins contain a large amount of glutamine- and proline-rich peptides which are not hydrolyzed by human digestive peptidases and can cause autoimmune celiac disease and other forms of gluten intolerance in predisposed people. Peptidases that efficiently cleave such immunogenic peptides can be used in enzyme therapy. The stored product insect pest Tribolium castaneum efficiently hydrolyzes gliadins. The main digestive peptidase of T. castaneum is cathepsin L, which is from the papain C1 family with post-glutamine cleavage activity. We describe the isolation and characterization of T. castaneum recombinant procathepsin L (rpTcCathL1, NP_001164001), which was expressed in Pichia pastoris cells. The activation of the proenzyme was conducted by autocatalytic processing. The effects of pH and proenzyme concentration in the reaction mixture on the processing were studied. The mature enzyme retained high activity in the pH range from 5.0 to 9.0 and displayed high pH-stability from 4.0 to 8.0 at 20 °C. The enzyme was characterized according to electrophoretic mobility under native conditions, activity and stability at various pH values, a sensitivity to various inhibitors, and substrate specificity, and its hydrolytic effect on 8-, 10-, 26-, and 33-mer immunogenic gliadins peptides was demonstrated. Our results show that rTcCathL1 is an effective peptidase that can be used to develop a drug for the enzyme therapy of various types of gluten intolerance.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tribolium / Enfermedad Celíaca Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Suiza
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tribolium / Enfermedad Celíaca Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2022 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Suiza