Site-specific modification of positively-charged surfaces on human serum albumin by malondialdehyde
T Ishii, S Ito, S Kumazawa, T Sakurai… - Biochemical and …, 2008 - Elsevier
T Ishii, S Ito, S Kumazawa, T Sakurai, S Yamaguchi, T Mori, T Nakayama, K Uchida
Biochemical and biophysical research communications, 2008•ElsevierMalondialdehyde (MDA), a lipid peroxidation product, reacts with lysine residues in proteins.
Human serum albumin (HSA) is a major target of MDA-modification of serum proteins. To
identify, the modification sites of HSA by MDA in vitro, MDA-treated HSA was digested with a
protease and the resulting peptides were subjected to liquid chromatography-tandem mass
spectrometry. We identified six peptides, which contained a N-propenal adduct at Lys136,
Lys174, Lys240, Lys281, Lys525, and Lys541, and revealed that Lys525 is the most reactive …
Human serum albumin (HSA) is a major target of MDA-modification of serum proteins. To
identify, the modification sites of HSA by MDA in vitro, MDA-treated HSA was digested with a
protease and the resulting peptides were subjected to liquid chromatography-tandem mass
spectrometry. We identified six peptides, which contained a N-propenal adduct at Lys136,
Lys174, Lys240, Lys281, Lys525, and Lys541, and revealed that Lys525 is the most reactive …
Malondialdehyde (MDA), a lipid peroxidation product, reacts with lysine residues in proteins. Human serum albumin (HSA) is a major target of MDA-modification of serum proteins. To identify, the modification sites of HSA by MDA in vitro, MDA-treated HSA was digested with a protease and the resulting peptides were subjected to liquid chromatography-tandem mass spectrometry. We identified six peptides, which contained a N-propenal adduct at Lys136, Lys174, Lys240, Lys281, Lys525, and Lys541, and revealed that Lys525 is the most reactive residue for MDA modification. Analysis of electrostatic surface potential of a 3-D model structure of HSA indicates that Lys525 is located at the center of positively charged grooves. The results of this study indicate that the modification of proteins by lipid-derived aldehydes may be influenced by the electrostatic potential of the protein surface.
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