Low-density lipoproteins (LDLs), the physiological vehicles for lipids, are potentially useful drug delivery devices for (hydrophobic) drugs. The physicochemical characteristics of LDL loaded with the adriamycin derivative AD 32 or the N-mustard derivative WB 4291 were compared to that of native and reconstituted LDL at different temperatures. X-ray solution scattering indicates that loading with AD 32 has no detectable effect on the particle structure at room temperature, in contrast to WB 4291. According to 19F NMR data, AD 32 molecules are located in two distinct chemical environments with restricted motional freedom of the CF3 groups in samples stored as lyophilisates. 1H NMR signals from AD 32 were not observed, while those from WB 4291 could be distinguished from those of LDL constituents. WB 4291 molecules are in an environment with a higher motional freedom than AD 32 molecules. 1H NMR data suggest a higher fluidity of the core components for the WB-loaded LDLs compared to the other LDL preparations. While the motional freedom of the phospholipid head groups seems to be temperature independent, there is an increase in the mobility of the lipid components in the core region of the LDL particles with temperature.