Abstract
cw-Diamminedichloroplatinum(II) ( cis-DDP) cleaved disulfide (S-S) bonds in human serum albumin (HSA) and brought about alterations of the secondary structure. The α-helix content decreased from 50.5% (native) to approx. 33% (four S-S bonds cleaved). The tendency toward a decrease corresponded only with an increase in the β-sheet. Sulfitolysis of the S-S bonds showed a tendency similar to that of metal binding. Fluorescence and UV difference spectra changed as a function of S-S bond cleavage and led to considerable differences between the two cleaving agents.
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