Study on the conformation changes of Lysozyme induced by Hypocrellin A: The mechanism investigation

Ma, Fei; Huang, Haihong; Zhou, Lin; Yang, Chao; Zhou, Jiahong; Liu, Zheng-Ming

doi:10.1016/j.saa.2012.07.136

Cited by 31 publications

(19 citation statements)

References 33 publications

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“…The double peaks for SPI also indicates that the 7s protein (peak at 308°C) shows a slightly faster degradation kinetics than 11s fraction (peak at 325°C), as described by Güttler . Some authors reported TGA profiles with thermal events at 294°C and 307°C for ovalbumin and lyzosyme, respectively, in agreement with the profiles reported in this study. The former authors also reported a moderate thermal event at 224°C that was attributed to some loss associated with ovalbumin melting.…”

Section: Resultssupporting

confidence: 91%

“…The temperature at maximum weight‐loss corresponding to moisture evaporation is 78.8°C and 94.7°C for SPI/GL and EW/GL, respectively. Subsequently, the weight loss that takes place during the second stage, from 130°C to 270°C or 275°C for SPI/GL and EW/GL, respectively, seem to be attributed to the evaporation of glycerol . Then, it is at higher temperatures when the protein degradation mainly occurs, with a maximum at a temperature around 300°C .…”

Section: Resultsmentioning

confidence: 97%

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Protein/glycerol blends and injection‐molded bioplastic matrices: Soybean versus egg albumen

Fernández‐Espada

Bengoechea

Cordobés

et al. 2015

J of Applied Polymer Sci

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Two well‐known proteins have been selected in order to produce bioplastics through injection molding: a soy protein isolate (SPI) and an egg white albumen concentrate (EW). Each of them has been thoroughly mixed with glycerol (40 wt %) and the blend then obtained have been characterized by means of rheological and thermomechanical techniques, which allowed the optimization of the processing moulding conditions (cylinder temperature, 60°C–65°C; mould temperature, 120°C; post‐injection pressure, 500–600 bars). Once bioplastics were obtained, their thermomechanical and tensile properties, as well as their water uptake capacity and transparency were evaluated. Bioplastics containing EW showed higher values in the elastic and loss moduli, E′ and E″, from −30°C to 130°C, than the corresponding SPI bioplastic. However, they both showed qualitatively the same evolution with temperature, where E′ and E″ decreased up to a plateau at high temperatures. When examining their tensile and water uptake properties is found that SPI bioplastics are more ductile and present enhanced water uptake behavior over EW bioplastics, which on the other hand possess higher Young's modulus. SPI seems to provide tougher bioplastics, being an excellent option for potential superabsorbent applications, whereas EW would suit for those applications requiring higher mechanical properties. © 2015 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2016, 133, 42980.

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Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 97%

Protein/glycerol blends and injection‐molded bioplastic matrices: Soybean versus egg albumen

Fernández‐Espada

Bengoechea

Cordobés

et al. 2015

J of Applied Polymer Sci

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“…As compared with native lysozyme, the peak positions of lysozyme–TBO system moved from 1657 cm −1 to 1655 cm −1 along with the amide‐II band shifted from 1542 to 1535 cm −1 (Fig. B), clearly indicating that TBO has induced considerable secondary structural changes in lysozyme . Gaussian multipeak fitting techniques are utilized to deconvoluting amide‐I band .…”

Section: Resultsmentioning

confidence: 98%

Elucidation of Binding Mechanism of Photodynamic Therapeutic Agent Toluidine Blue O with Chicken Egg White Lysozyme by Spectroscopic and Molecular Dynamics Studies

Shanmugaraj

Umadevi

Lakshmipathi

et al. 2017

Photochem & Photobiology

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The nature of binding mechanism of toluidine blue O (TBO) with chicken egg white lysozyme was studied comprehensively by various spectroscopic and computational methods. Both steady state and time-resolved fluorescence studies unambiguously point to the prevalence of static quenching mechanism in lysozyme-TBO system. Thermodynamic parameters revealed that the association of TBO with lysozyme was a spontaneous process in which hydrophobic and hydrogen bond interactions played a pivotal role in the binding process. The secondary and tertiary conformational changes of lysozyme in the presence of TBO were unraveled using absorption, Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD) techniques. Molecular docking studies of lysozyme-TBO system substantiated the findings of site marker experiment and revealed TBO adjacent to Trp-63 and Trp-108 residues of lysozyme. Molecular dynamics (MD) simulation studies of lysozyme-TBO system indicate a stable and effective complexation of TBO with lysozyme. It is hoped that the results presented here will enable further understanding of TBO toxicity.

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“…Figure shows a spectral overlap between the fluorescence emission spectrum of BSA and the UV/vis absorption spectrum of ZnPc. A spectrum ranging from 300 to 500 nm was chosen to calculate the overlap integral and average distance between BSA and ZnPc using eqns :

E = \frac{{R_{0}}^{6}}{{R_{0}}^{6} + r^{6}} = 1 - \frac{F}{F_{0}}

…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic study on the interaction of bovine serum albumin with zinc(II) phthalocyanine

Wang

et al. 2015

Luminescence

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The interaction between the photosensitive antitumour drug, 2(3),9(10),16(17),23(24)-tetra-(((2-aminoethylamino)methyl)phenoxy)phthalocyaninato-zinc(II) (ZnPc) and bovine serum albumin (BSA) has been investigated using various spectroscopic methods. This work may provide some useful information for understanding the interaction mechanism of anticancer drug-albumin binding and gain insight into the biological activity and metabolism of the drug in blood. Based on analysis of the fluorescence spectra, ZnPc could quench the intrinsic fluorescence of BSA and the quenching mechanism was static by forming a ground state complex. Meanwhile, the Stern-Volmer quenching constant (KSV), binding constant (Kb), number of binding sites (n) and thermodynamic parameters were obtained. Results showed that the interaction of ZnPc with BSA occurred spontaneously via hydrogen bond and van der Waal's force. According to Foster's non-radioactive energy transfer theory, the energy transfer from BSA to ZnPc occurred with high possibility. Synchronous fluorescence and circular dichroism (CD) spectra also demonstrated that ZnPc induced the secondary structure of and conformation changes in BSA, especially α helix.

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Study on the conformation changes of Lysozyme induced by Hypocrellin A: The mechanism investigation

Cited by 31 publications

References 33 publications

Protein/glycerol blends and injection‐molded bioplastic matrices: Soybean versus egg albumen

Protein/glycerol blends and injection‐molded bioplastic matrices: Soybean versus egg albumen

Elucidation of Binding Mechanism of Photodynamic Therapeutic Agent Toluidine Blue O with Chicken Egg White Lysozyme by Spectroscopic and Molecular Dynamics Studies

Spectroscopic study on the interaction of bovine serum albumin with zinc(II) phthalocyanine

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