[Conformational analysis of cysteine-containing peptides and prospects of their application to 213Bi chelating in antitumor therapy].
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.
Gogitidze
T V
TV
Demushkin
V P
VP
Zhavoronkova
E V
EV
Kopytov
V V
VV
Marchenkov
N S
NS
D000818:Animals; D001729:Bismuth / Q000737:chemistry* / Q000627:therapeutic use; D002614:Chelating Agents / Q000737:chemistry* / Q000627:therapeutic use; D003545:Cysteine / Q000737:chemistry*; D006801:Humans; D008956:Models, Chemical; D009369:Neoplasms / Q000737:chemistry / Q000000981:diagnostic imaging / Q000188:drug therapy; D010455:Peptides / Q000737:chemistry* / Q000627:therapeutic use; D017433:Protein Structure, Secondary; D011877:Radionuclide Imaging; D012984:Software
D002614:Chelating Agents; D010455:Peptides; D003545:Cysteine; D001729:Bismuth