Spectroscopic studies on the interaction of Ga3+-hypocrellin A with myoglobin

Xie, Wenli; Wei, Shaohua; Liu, Jihua; Ge, Xuefeng; Zhou, Lin; Zhou, Jiahong; Shen, Jian

doi:10.1016/j.saa.2013.10.085

Cited by 9 publications

(6 citation statements)

References 40 publications

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“…Such a phenomenon observed in the absorption spectra of Hb or Mb suggested that C3G interacted with the surface of Hb or Mb, and had no direct effect on its interior structure. The results were consistent with Xie et al (2014). In a word, these observations strongly suggested that binding interactions existed between C3G and BSA, Hb or Mb.…”

Section: Uv-vis Absorption Spectrasupporting

confidence: 84%

“…After the addition of C3G, the CD signal of BSA, Hb and Mb decreased markedly, indicating that the binding interaction of C3G with BSA, Hb or Mb induced changes in the secondary structures of the protein (Liu, Tian, Tian, Hu, & Chen, 2004). While the CD spectra of proteins are similar before and after conjugation, it is obvious that the structure of protein-C3G is still predominately a-helix (Xie et al, 2014). With the help of the CDNN program, the secondary structural elements of pure BSA, Hb or Mb and its conjugate system were calculated.…”

Section: Spectramentioning

confidence: 98%

“…For example, cyanidin-3-glucoside (C3G) exhibits free radical scavenging activity, suppresses inflammation, protects against endothelial dysfunction, vascular failure and myocardial damage, prevents obesity, ameliorates hyperglycemia and seems to help prevent cardiovascular disease (Kähkönen & Heinonen, 2003;Noda, Kaneyuki, Mori, & Packer, 2002;Seeram, Momin, Nair, & Bourquin, 2001;Serraino et al, 2003;Tsuda, Horio, Uchida, Aoki, & Osawa, 2003;Xu, Ikeda, & Yamori, 2004). In order to be transferred into a tumor, C3G needs to be bound by various proteins after ingestion, so knowing the details of the binding characteristics of C3G with these proteins in the therapeutic procedure at molecular level is of great importance (Xie et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Interaction of cyanidin-3-O-glucoside with three proteins

Tang

et al. 2016

Food Chemistry

121

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Section: Uv-vis Absorption Spectrasupporting

confidence: 84%

Section: Spectramentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Interaction of cyanidin-3-O-glucoside with three proteins

Tang

et al. 2016

Food Chemistry

121

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“…Because Trp is known to exhibit multi‐exponential decays , lifetime measurement of BSA was carried out by exciting the sample at 265 nm to excite the donor only. In time‐resolved fluorescence analysis, the residual plot, as well as χ 2 value, indicated that the fluorescence decay profiles of Trp were bi‐exponential in nature .…”

Section: Resultsmentioning

confidence: 99%

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

Wang

et al. 2015

Luminescence

Self Cite

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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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“…The results (Table 2) suggest that the α-helical content of native Mb is 65% and its corresponding β-sheet content is 6.8%, which is consistent with the literature report. 54 The presence of C m −E2O−C m led to a noticeable decrease and increase in the respective α-helical and β-sheet contents of Mb, relative to its pure state, signifying an obliteration of its secondary structure. Even after the addition of the concerned cationic geminis, shape of CD spectra remains almost similar, which reveals that Mb still have predominant α-helical content.…”

Section: Industrial and Engineering Chemistry Researchmentioning

confidence: 97%

Multifaceted Analysis of the Noncovalent Interactions of Myoglobin with Finely Tuned Gemini Surfactants: A Comparative Study

Akram

Anwar

Bhat

et al. 2017

Ind. Eng. Chem. Res.

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This work unveils the noncovalent interactions of a novel series of finely tuned gemini surfactants (C m –E2O–C m , m = 12, 14, and 16) with myoglobin (Mb) using multifaceted spectroscopic/voltammetric and docking techniques. The Mb-binding capacity of these geminis decreased in the order of C14–E2O–C14 > C16–E2O–C16 > C12–E2O–C12, following the 1:2 stoichiometry, as confirmed by the quantitative evaluation of binding constants via intrinsic fluorescence and cyclic voltammetry. The binding-induced microenvironmental and conformational changes of Mb were explored by pyrene/synchronous/three-dimensional (3-D) fluorescence and absorption spectroscopy. Furthermore, far- and near-ultraviolet (UV) circular dichroism spectral results depicted discernible changes in both secondary and tertiary structures of Mb upon complexation with C m –E2O–C m . Molecular docking specified the binding site, and aromatic residues involved in the complexation. These investigations provide deeper insight into the structure–property relationships of biomacromolecules, and they will be useful in designing/selecting appropriate surfactants which, in turn, can facilitate the application of protein–surfactant mixtures in pharmaceutical, biological, and industrial fields.

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Spectroscopic studies on the interaction of Ga3+-hypocrellin A with myoglobin

Cited by 9 publications

References 40 publications

Interaction of cyanidin-3-O-glucoside with three proteins

Interaction of cyanidin-3-O-glucoside with three proteins

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

Multifaceted Analysis of the Noncovalent Interactions of Myoglobin with Finely Tuned Gemini Surfactants: A Comparative Study

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