Chiroptical methods are widely used in structural and conformational analyses of biopolymers. The application of these methods to investigations of biofluids would provide new avenues for the molecular diagnosis of protein-misfolding diseases. In this work, samples of human blood plasma and hen egg white were analyzed using a combination of conventional and chiroptical methods: ultraviolet absorption/electronic circular dichroism (UV/ECD), Fourier transform infrared absorption/vibrational circular dichroism (FTIR/VCD), and Raman scattering/Raman optical activity (Raman/ROA). For comparison, the main components of these substances—human serum albumin (HSA) and ovalbumin (Ova)—were also analyzed by these methods. The ultraviolet region of the ECD spectrum was analyzed using the CDNN CD software package to evaluate the secondary structures of the proteins. The UV/ECD, FTIR/VCD, and Raman/ROA spectra of the substances were quite similar to those of the corresponding major proteins, while some differences were also detected and explained. The conclusions drawn from the FTIR/VCD and Raman/ROA data were in good agreement with the secondary structures calculated from ECD. The results obtained in this work demonstrate that the chiroptical methods used here can be applied to analyze not only pure protein solutions but also more complex systems, such as biological fluids.

Analysis of human blood plasma and hen egg white by chiroptical spectroscopic methods (ECD, VCD, ROA)

Thermostabilization of a thermophilic 1,4-α-glucan branching enzyme through C-terminal truncation.

The clinical use of daunomycin is restricted by dose-dependent toxicity and low specificity against cancer cells. In the present study, modified superparamagnetic iron oxide nanoparticles were employed to load daunomycin and the drug-loaded nanospheres exhibited satisfactory size and smart pH-responsive release. The cellular uptake efficiency, targeted cell accumulation, and cell cytotoxicity experimental results proved that the superparamagnetic iron oxide nanoparticle-loading process brings high drug targeting without decreasing the cytotoxicity of daunomycin. Moreover, a new concern for the evaluation of nanophase drug delivery's effects was considered, with monitoring the interactions between human serum albumin and the drug-loaded nanospheres. Results from the multispectroscopic techniques and molecular modeling calculation elucidate that the drug delivery has detectable deleterious effects on the frame conformation of protein, which may affect its physiological function.

Daunomycin-loaded superparamagnetic iron oxide nanoparticles: Preparation, magnetic targeting, cell cytotoxicity, and protein delivery research:

A novel method for enhanced circular dichroism (CD) detection is proposed based on a surface plasmon resonance (SPR) prism coupler and a polarization scanning ellipsometry technique. An analytical model is derived to extract the CD and degree of polarization (DOP) properties of optical samples with and without scattering effects, respectively. The validity of the analytical model is confirmed by means of numerical simulations. The simulation results show that the proposed detection method has a sensitivity of 10-5~10-6 RIU (refractive index unit) for refractive indices in the range of 1.32~1.36 and 1.3100~1.3118. The practical feasibility of the proposed method is demonstrated by the experimental results for the sensitivity of the CD with the chlorophyllin samples with/without scattering effect. It is shown that for both types of sample, the extracted CD value increases linearly with the chlorophyll concentration over the considered range. In general, the results obtained in this study show that the measured CD response is highly sensitive to the polarization scanning angle. Consequently, the potential of polarization scanning ellipsometry for high-resolution CD detection is confirmed.

Surface plasmon resonance prism coupler for enhanced circular dichroism sensing.

In spite of the importance of anisotropic circular dichroism, in practice, it is difficult to get rid of the artifacts that arise from the imperfection of the circular polarization. Undesirable linear dichroism, interference of two orthogonal polarization states, and linear birefringence prevent us from making accurate measurements. We propose a theoretical method for evaluating the contributions of the first two, which are thought to be the main artifacts when specimens are not thick enough. Using the time-dependent perturbation theory and taking into account the direction of light propagation toward an orientationally fixed molecule, we formulated the transition probability of systems perturbed by arbitrarily polarized light and the absorption difference associated with two kinds of polarized light. We also formulated, as an extension of the dissymmetry factor of circular dichroism, a newly defined dissymmetry factor associated with two arbitrary polarization states. Furthermore, we considered a mixed-state of photon ensemble in which polarization states distribute at a certain width around a certain average. Although the purity of polarization and ellipticity does not correspond immediately, by considering the mixed state it is possible to treat them consistently. We used quantum statistical mechanics to describe the absorption difference for two kinds of photon ensembles and applied the consequent formula to examine the reported experimental results of single-molecule chiroptical responses under discussion in the recent past. The artifacts are theoretically suggested to be sensitive to the incident direction of elliptically polarized light and to the oriented systems, the ellipticity, and the orientation of ellipse. The mixed state has little, if any, effect when the polarization state distribution is narrow.

Anisotropic elliptical dichroism and influence of imperfection of circular polarization upon anisotropic circular dichroism

A sensitive method based on fluorescence-detected circular dichroism for protein local structure analysis

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A sensitive method based on fluorescence-detected circular dichroism for protein local structure analysis