Abstract
Molecular modeling has been employed to study the interaction of hypericin (Hyp) with human serum albumin (HSA). The structural model for Hyp/HSA complex is presented. Our results indicate that Hyp is bound in II A subdomain of HSA close to the tryptophan 214 (Trp214) (distance 5.12 Å between the centers of masses). In the presented model the carbonyl group of Hyp is hydrogen bonded to the Asn458. Another two candidates for hydrogen bonds have been identified between the bay-region hydroxyl group of Hyp and the carbonyl group of the Trp214 peptidic link and between the peri-region hydroxyl group of Hyp and Asn458 carbonyl group.
Highlights
Hypericin (Figure 1) is a natural photosensitizing polycyclic aromatic dione, which can be extracted from plants of the Hypericum genus [1]
Timeresolved spectroscopy has been used in our later study of the human serum albumin (HSA)-hypericin (Hyp/HSA) complex, in which we have shown that Hyp is rigidly held in the IIA subdomain and is situated very close to tryptophan 214 (Trp214) [16]
SERS quenches the fluorescence of Hyp and a behaviour of Hyp in the complex with HSA can be detected
Summary
Hypericin (Figure 1) is a natural photosensitizing polycyclic aromatic dione, which can be extracted from plants of the Hypericum genus [1]. It displays virucidal activity against several types of viruses, including the human immunodeficiency virus (HIV), [2,3,4] as well as antiproliferative and cytotoxic effects on tumor cells [5,6,7]. Other important biological properties of Hyp have been described, such as potent antidepressive activity [9], light-dependent inhibition of protein kinase C [5, 10], tyrosine kinase [11] and mitochondrial succinoxidase activity [12]. Biological activity of Hyp and related compounds has been reviewed by Diwu et al [13]
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