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

✍ Scribed by Bo Zhou; Zhi Zhang; Yue Zhang; Ran Li; Qi Xiao; Yi Liu; ZaoYing Li

Publisher: John Wiley and Sons
Year: 2009
Tongue: English
Weight: 205 KB
Volume: 98
Category: Article
ISSN: 0022-3549
DOI: 10.1002/jps.21413

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✦ Synopsis

The interaction between cationic porphyrin, a potential valuable antitumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (K SV ¼ (3.24 AE 0.29) Â 10 4 M À1 ) and surface plasmon resonance (SPR) spectroscopy (K A ¼ (6.287 AE 0.407) Â 10 4 M À1 ). The association rate constant (k a ¼ 1622 AE 72.9 M À1 s À1 ) and dissociation rate constant (K d ¼ 0.02589 AE 0.0024 s À1 ) 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.

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