Conformational analysis of cysteine-containing peptides and prospects of their application to 213Bi chelating in antitumor therapy |
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| Authors: | T. V. Gogitidze V. P. Demushkin E. V. Zhavoronkova V. V. Kopytov N. S. Marchenkov |
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| Affiliation: | (1) Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia;(2) Russian Scientific Center Kurchatov Institute, pl. Kurchatova 1, Moscow, 123182, Russia |
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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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| Keywords: | chelators conformational analysis of peptides metallothioneins phytochelatins radionuclides |
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