N-terminal deletion affects catalytic activity of saporin toxin
| Autor: | Francesca Bonini, Giulio Fracasso, Roberta Traini, Mauro Dalla Serra, Fabrizio Comper, Marco Colombatti, Rossella Tomazzolli |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Saporin
Mutant Cell Biology medicine.disease_cause Biochemistry Catalysis Protein Structure Secondary Substrate Specificity Cell Line Tumor medicine Humans Protein Isoforms Cytotoxic T cell Cytotoxicity Molecular Biology Protein secondary structure Toxin Immunotoxins Ribosome-inactivating protein Membranes Artificial Cell Biology Molecular biology medicine.anatomical_structure Protein Biosynthesis Mutation biology.protein Colorimetry Gene Deletion |
| Zdroj: | Journal of cellular biochemistry 98 (2006): 1130–1139. doi:10.1002/jcb.20845 info:cnr-pdr/source/autori:Bonini F., Traini R., Comper F., Fracasso G., Tomazzolli R., Dalla Serra M., Colombatti M./titolo:N-terminal deletion affects catalytic activity of saporin toxin./doi:10.1002%2Fjcb.20845/rivista:Journal of cellular biochemistry (Print)/anno:2006/pagina_da:1130/pagina_a:1139/intervallo_pagine:1130–1139/volume:98 |
| ISSN: | 1097-4644 0730-2312 |
| Popis: | Single-chain ribosome inactivating proteins (RIPs) are cytotoxic components of macromolecular pharmaceutics for immunotherapy of cancer and other human diseases. Saporin belongs to a family of single-chain RIPs sharing sequence and structure homology. In a preliminary attempt to define an active saporin polypeptide of minimum size we have generated proteins with deletions at the N-terminus and at the C-terminus. An N-terminal (sapΔ1–20) deletion mutant of saporin displayed defective catalytic activity, drastically reduced cytotoxicity but increased ability to interact with liposomes inducing their permeabilization at low pH. A C-terminal (sapΔ239–253) deletion mutant showed instead a moderate reduction in cytotoxic activity. A substantial alteration of secondary structure was evidenced by Fourier transformed infrared spectroscopy (FTIR) in the sapΔ1–20 mutant. It can be hypothesized that the defective functions of sapΔ1–20 are due to alterations of its spatial configuration. J. Cell. Biochem. 98: 1130–1139, 2006. © 2006 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text