[Spectroscopic studies on the formation of metal complexes and on the protein binding of antiviral thiosemicarbazone derivatives (author's transl)].
The complexation of some thiosemicarbazones and isothiosemicarbazones of isatin and quinolin-2-aldehydes with Cu2+, Zn2+ and Mn2+ ions was spectrometrically investigated. Semiquantitative data, obtained from extinction values, about the relative complexing tendencies within some groups of homologous substances were brought in relation to their antiviral effects and binding to bovine serum albumin. The complexing tendencies were greatest in compounds with methyl substituents and decreased for higher alkyl substituents. whereas the binding to protein increased in the same order. The well-known maxima of the antiviral observed with medium alkyl groups may be explained by a superposition of these effects.
D000998:Antiviral Agents / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism; D013056:Spectrophotometry, Ultraviolet; D013882:Thiosemicarbazones / Q000378:metabolism*
D000998:Antiviral Agents; D008670:Metals; D012709:Serum Albumin; D013882:Thiosemicarbazones
Spektroskopische Untersuchungen zur Metallkomplexbildung und Proteinbindung antiviraler Thiosemicarbazonderivate.