Article

Binding of cationic porphyrin to human serum albumin studied using comprehensive spectroscopic methods.

State Key Laboratory of Virology, Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Journal of Pharmaceutical Sciences (impact factor: 3.06). 06/2008; 98(1):105-13. DOI:10.1002/jps.21413 pp.105-13
Source: PubMed

ABSTRACT The interaction between cationic porphyrin, a potential valuable anti-tumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (K(SV) = (3.24 +/- 0.29) x 10(4) M(-1)) and surface plasmon resonance (SPR) spectroscopy (K(A) = (6.287 +/- 0.407) x 10(4) M(-1)). The association rate constant (k(a) = 1622 +/- 72.9 M(-1) s(-1)) and dissociation rate constant (K(d) = 0.02589 +/- 0.0024 s(-1)) of the binding process were also calculated. Compared with the two results, it was known that one of the binding sites was near the tryptophan residue and also there existed other binding sites. The Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy indicated that the confirmation of HSA was nearly not affected with the addition of porphyrin.

0 0
 · 
0 Bookmarks
 · 
27 Views
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.

Keywords

association rate constant
 
binding constants
 
binding process
 
binding sites
 
cationic porphyrin
 
dissociation rate constant
 
fluorescence quenching method
 
human serum albumin
 
infrared
 
porphyrin
 
spectroscopy methods
 
SPR
 
surface plasmon resonance
 
tryptophan residue
 
two results
 

Bo Zhou