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The interaction of UCPs with CT DNA are studied in detail by zeta potential, Energy dispersive spectrometer (EDS) spectroscopy, Thermogravimetric (TGA) analysis, DNA melting determination and various spectroscopic techniques including Ultraviolet–Visible (UV–Vis) absorption, fluorescence, circular dichroism (CD), Fourier transform infrared (FTIR) and Raman spectroscopy. The results indicate that CT DNA can assemble on the surface of UCPs mainly by relative stronger hydrophobic force and electrostatic binding, and the predominant interaction site is the deoxyribosyl phosphate backbone of CT DNA. Moreover, after interacting with UCPs, the double helix structure of DNA is undamaged.

The UV-vis absorption, steady state/time resolved fluorescence spectroscopy and synchronous fluorescence, circular dichroism (CD) spectroscopy are used to investigate the interaction mechanisms of dihydroartemisinin (DHA) and 9-hydroxy-dihydroartemisinin (9-OH DHA), respectively. The UV-vis studies present that DHA and 9-OH DHA can disturb the structure of bovine hemoglobin (BHb). Steady state/time resolved and synchronous fluorescence spectroscopy reveal that the binding constant of DHA with BHb is bigger than 9-OH DHA. CD spectra indicate DHA and 9-OH DHA can change the conformation of BHb. The comparison results suggest that the binding of BHb with DHA is more stable and stronger than 9-OH DHA.

In this article, the interaction mechanism of Ga 3+ -hypocrellin A (Ga 3+ –HA) with myoglobin (Mb) is studied in detail through various spectroscopic technologies. UV–vis absorption and fluorescence spectra demonstrate the interaction process. The Stern–Volmer plot and the time-resolved fluorescence study suggest the fluorescence quenching mechanism of Mb by Ga 3+ –HA is a static quenching procedure, and the electronic transfer forces play a major role in binding Ga 3+ –HA to Mb. Furthermore, synchronous fluorescence studies and circular dichroism (CD) spectra reveal that the conformation of Mb is changed after its conjugation with Ga 3+ –HA.

In this study, the chelation of Hypocrellin A (HA) with Al 3+ in water solution has been synthesized, and the interactions of HA and Al 3+ –HA complex with calf thymus DNA are in detail compared by UV–vis and fluorescence spectroscopic techniques, circular dichroism spectroscopy and viscosity measurement. The experiment results suggest that HA and Al 3+ –HA complex both could bind to CT DNA by intercalation mode, and double helix of DNA was damaged. Moreover, Al 3+ –HA complex not only displays higher absorption at therapeutic window but also displays stronger binding affinity to CT DNA than HA.

A novel 3-(4-methoxybenzylamino) propanoic acid substituted water-soluble zinc phthalocyanine (CNPcZn) was synthesized. The interaction between CNPcZn with calf thymus DNA (CT DNA) was studied using spectroscopic methods. The studies indicated that CNPcZn has strong affinity to CT DNA, and furthermore, CNZnPc showed excellent photodamaging activity to CT DNA. Above results indicated that such CNPcZn has great potential to be used as an effective photosensitizer in the field of photodynamic therapy.

The UV-vis, steady state/time resolved fluorescence spectroscopy and circular dichroism spectroscopy are employed to investigate the interaction mechanisms of Al(13)-Hb and Al(III)-Hb, respectively. The UV-vis studies represent that Al(13) and Al(III) could directly disturb the structure of Hb and induce the heme group exposed to the aqueous medium. Steady state/time resolved and synchronous fluorescence spectroscopy reveal that Al(13) and Al(III) can change the polarity around the fluorophore molecule of Hb. Al(13) makes the protein unfolding and Al(III) induces the protein buried inside the structure. The interaction processes are static quenching mechanisms and the main forces are electrostatic interactions. Moreover, circular dichroism spectra display Al(13) makes greater effect than Al(III), which is reflected on the degrees of α-helix of Hb. The comparison results suggest that Al(13) displays stronger toxicity.

The interactions between Lysozyme and Hypocrellin A are investigated in details using time-resolved fluorescence, fourier transform infrared spectroscopy (FTIR), circular dichroism spectroscopy (CD), three-dimensional fluorescence spectra, and thermal gravimetric analysis (TGA) techniques. The results of time-resolved fluorescence suggest that the quenching mechanism is static quenching. FTIR and CD spectroscopy provide evidences of the reducing of α-helix after interaction. Hypocrellin A could change the micro-environmental of Lysozyme according to hydrophobic interaction between the aromatic ring and the hydrophobic amino acid residues, and the altered polypeptide backbone structures induce the reduction of α-helical structures. Moreover, TGA study further demonstrates the structure changes of Lysozyme on the effect of Hypocrellin A. This study could provide some important information for the derivatives of HA in pharmacy, pharmacology and biochemistry.

The spectrophotometric and spectrofluorimetric studies revealed that hemoglobin (Hb) could interact with hypocrellin A, a photosensitizing drug used in photodynamic therapy. It was found that this kind of interaction can induce the conformational changes in Hb. In addition, based on fluorescence quenching titration and electron paramagnetic resonance spectroscopy results, the binding parameters, thermodynamic parameters are obtained. The quenching mechanism is also proposed.