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Conformational analysis of cysteine-containing peptides and prospects of their application to 213Bi chelating in antitumor therapy

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Abstract

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)3-Asp, (Cys-Gly)3-Glu, (Cys-βAla)3, (Cys-γGlu)3, and (Cys-Gly-Gly)3. All the possible low-energy conformations of the molecules were revealed and the role of intra-and interresidual 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-βAla)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, or Gly) were revealed. In the α-helical conformations of these pentapeptides, the distance between the sulfur atoms corresponds to that in Bi2S3.

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Abbreviations

ECEPP:

Empirical Conformational Energy Program for Peptides

SP:

solubility product

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Correspondence to V. P. Demushkin.

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Original Russian Text © T.V. Gogitidze, V.P. Demushkin, E.V. Zhavoronkova, V.V. Kopytov, N.S. Marchenkovv, 2006, published in Bioorganicheskaya Khimiya, 2006, Vol. 32, No. 3, pp. 268–275.

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Gogitidze, T.V., Demushkin, V.P., Zhavoronkova, E.V. et al. Conformational analysis of cysteine-containing peptides and prospects of their application to 213Bi chelating in antitumor therapy. Russ J Bioorg Chem 32, 240–247 (2006). https://doi.org/10.1134/S1068162006030058

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  • DOI: https://doi.org/10.1134/S1068162006030058

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