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.

中文翻译：

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使用综合光谱法研究阳离子卟啉与人血清白蛋白的结合

使用光谱学方法研究了阳离子卟啉（一种潜在的有价值的抗肿瘤和抗生素药物）与人血清白蛋白（HSA）之间的相互作用。使用荧光猝灭法（K（SV）=（3.24 +/- 0.29）x 10（4）M（-1））和表面等离振子共振（SPR）光谱获得结合常数（K（A）=（6,287 + /-0.407）x 10（4）M（-1））。结合的缔合速率常数（k（a）= 1622 +/- 72.9 M（-1）s（-1））和解离速率常数（K（d）= 0.02589 +/- 0.0024 s（-1））过程也进行了计算。与两个结果相比，已知结合位点之一靠近色氨酸残基，并且还存在其他结合位点。