Investigating the binding of curcumin derivatives to bovine serum albumin.
The interaction of bovine serum albumin (BSA) with isoxazolcurcumin (IOC) and diacetylcurcumin (DAC) has been investigated. Binding constants obtained were found to be in the 10(5) M(-1) range. Minor conformational changes of BSA were observed from circular dichroism (CD) and Fourier transformed infrared (FT-IR) studies on binding. Based on Förster's theory of non-radiation energy transfer, the average binding distance, r between the donor (BSA) and acceptors IOC and DAC was found to be 3.79 and 4.27 nm respectively. Molecular docking of isoxazolcurcumin and diacetylcurcumin with bovine serum albumin indicated that they docked close to Trp 213, which is within the hydrophobic subdomain.
Sahoo
Bijaya Ketan
BK
Department of Chemistry, Indian Institute of Technology, Kharagpur, India.
Ghosh
Kalyan Sundar
KS
Dasgupta
Swagata
S
D000818:Animals; D001665:Binding Sites; D002942:Circular Dichroism; D003474:Curcumin / Q000031:analogs & derivatives / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D004735:Energy Transfer; D057927:Hydrophobic and Hydrophilic Interactions; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared
D012710:Serum Albumin, Bovine; C493686:diacetylcurcumin; D003474:Curcumin