Conformational analysis of cysteine-containing peptides and prospects of their application to 213Bi chelating in antitumor therapy
| Autor: | N. S. Marchenkov, E. V. Zhavoronkova, V. V. Kopytov, V. P. Demushkin, T. V. Gogitidze |
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| Rok vydání: | 2006 |
| Předmět: |
animal structures
Stereochemistry chemistry.chemical_element Peptide Biochemistry Pentapeptide repeat Protein Structure Secondary Neoplasms Animals Humans Bioorganic chemistry Molecule Chelation Cysteine Radionuclide Imaging Chelating Agents chemistry.chemical_classification integumentary system Chemistry Organic Chemistry Sulfur Antitumor therapy Models Chemical Peptides Bismuth Software |
| Zdroj: | Russian Journal of Bioorganic Chemistry. 32:240-247 |
| ISSN: | 1573-9163 1068-1620 |
| DOI: | 10.1134/s1068162006030058 |
| Popis: | The method of conformational analysis was applied to the spatial structures of peptide analogues of phytochelatins and some fragments of metallothioneins: (Cys-Gly)3, (Cys-Gly)3Asp, (Cys-Gly)3Glu, (Cys-betaAla)3, (Cys-gammaGlu)3, and (Cys-Gly-Gly)3. All the possible low-energy conformations of the molecules were revealed and the role of intra- and inter-residual interactions in the formation of their spatial structures was determined. A different tendency of the molecules under study for acceptance of conformations favorable for binding bismuth ions was shown. Low-energy structures providing an optimum binding of bismuth ion were shown to be most frequent for (Cys-betaAla)3 peptide. Among the analogues of peptide fragments of the metallothioneins, lacking in natural peptides, low-energy pentapeptide CCXXC fragments (where X = Gln, Asn, Phe, Tyr, and Gly) were revealed. In the alpha-helical conformations of these pentapeptides, the distance between the sulfur atoms corresponds to that in Bi2S3. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2006, vol. 32, no. 3; see also http://www.maik.ru. |
| Databáze: | OpenAIRE |
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