Citation: WANG Li-Na, LI Shuang, HUANG Fu-Ping, YU Qing, BIAN He-Dong, CHEN Zhen-Feng, LIANG Hong. Conformational Changes of Human Serum Albumin by Plumbagin in Presence of Cu2+ or Mn2+[J]. Chinese Journal of Inorganic Chemistry, ;2014, 30(5): 1151-1159. doi: 10.11862/CJIC.2014.027
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Circular dichroism (CD) and Raman spectroscopy were employed to investigate the binding of plumbagin (PLU) to human serum albumin (HSA) in the presence of Cu2+ or Mn2+. The results indicate that PLU changes the secondary structure of HSA and reduces the α-helix content. The binding of PLUalso causes the conformational changes of disulfide bridges and the microenvironment of Tyr, Trp residues. In the presence of the metal ion (Cu2+or Mn2+), the above changes are gradually strengthened.
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