Nucleophilic scission of thioester linkages and conformational changes in human plasma low density lipoproteins.

A comparison between conformations of native and methylamine modified human plasma low density lipoproteins (hydrated density 1.032-1.043 g/ml) has been presented. Near UV circular dichroism and difference absorption spectra of modified low density lipoprotein have suggested substantial differences in the local environments of several aromatic amino acid side chains. Relatively lower ellipticity at 222 nm of modified lipoprotein indicated alterations in the secondary structures of its protein moiety. Nucleophilic reaction of methylamine did not cause the peptide bond scission but it brought conformational transition such that some of the buried hydrophobic domains of the protein moiety got exposed to the aqueous environment.