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Spectroscopic investigations on the binding of an iodinated chlorin p6-copper complex to human serum albumin
Photochemical & Photobiological Sciences ( IF 3.1 ) Pub Date : 2017-10-16 00:00:00 , DOI: 10.1039/c7pp00197e
P. Sarbadhikary 1, 2, 3, 4, 5 , A. Dube 1, 2, 3, 4, 5
Affiliation  

The insertion of suitable metals or high Z elements in tumour-avid tetrapyrrole compounds is a promising approach to obtain potential agents for multimodal cancer therapeutics and tumour imaging. Using chlorin p6, a chlorophyll derivative, we synthesized a novel iodinated chlorin p6-copper complex (ICp6-Cu) that can be applied to the photodynamic therapy and photon activation therapy of cancer. In the present study, we investigated the interaction of ICp6-Cu with human serum albumin (HSA) using UV-Vis absorption and fluorescence spectroscopy. The addition of HSA to ICp6-Cu at physiological pH led to a ∼7 nm red shift in its Soret and Q band absorption. The binding constant (Kb) and the number of binding sites (n) of ICp6-Cu obtained from the quenching of the intrinsic fluorescence of HSA were 2.9 × 106 M−1 and 1.2 respectively. The distance between the Trp-214 residue and ICp6-Cu computed from Förster non-radiative energy transfer (FRET) theory was 3.1 nm. The emission of the ICp6-Cu fluorescence when excited at the protein’s Trp absorption (295 nm) further substantiated the FRET between the Trp residue and ICp6-Cu. Synchronous spectroscopy revealed that the quenching of protein Trp fluorescence was higher than that of Tyr with no significant shift in peak position. Results suggested that HSA acts as a carrier protein for ICp6-Cu with a high probability that the binding of ICp6-Cu occurred at subdomain IIA and the binding had no effect on the conformation of HSA.

中文翻译:

碘化二氢卟酚p 6-铜配合物与人血清白蛋白 结合的光谱研究

在肿瘤亲和的四吡咯化合物中插入合适的金属或高Z元素是获得用于多峰癌症治疗和肿瘤成像的潜在药物的有前途的方法。我们使用叶绿素衍生物二氢卟酚p 6合成了一种新型碘化的二氢卟酚p 6-铜配合物(IC p 6 -Cu),可用于癌症的光动力疗法和光子活化疗法。在本研究中,我们使用UV-Vis吸收和荧光光谱法研究了IC p 6 -Cu与人血清白蛋白(HSA)的相互作用。将HSA添加到IC6生理pH下的-Cu导致其Soret和Q带吸收发生约7 nm的红移。通过HSA的固有荧光的猝灭获得的IC p 6 -Cu的结合常数(K b)和结合位点数(n)分别为2.9×10 6 M -1和1.2。根据福斯特(Förster)非辐射能量转移(FRET)理论计算得出的Trp-214残留物与IC p 6 -Cu之间的距离为3.1 nm。当在蛋白质的Trp吸收(295 nm)处激发时,IC p 6 -Cu荧光的发射进一步证实了Trp残基和IC p 6之间的FRET。-铜 同步光谱显示,蛋白Trp荧光的猝灭高于Tyr的猝灭,峰位置无明显变化。结果表明,HSA充当IC p 6 -Cu的载体蛋白,很有可能IC p 6 -Cu结合发生在亚结构域IIA上,并且该结合对HSA的构象没有影响。
更新日期:2017-10-16
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