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Binding of citreoviridin to human serum albumin: multispectroscopic and molecular docking.

Hou H, Qu X, Li Y, Kong Y, Jia B, Yao X, Jiang B - Biomed Res Int (2015)

Bottom Line: Citreoviridin (CIT), a mycotoxin produced by Penicillium citreonigrum, is a common contaminant of wide range of agriproducts and detrimental to human and animal health.The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with hydrophobic and hydrogen bond force.Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via fluorescence resonance energy transfer method.

View Article: PubMed Central - PubMed

Affiliation: School of Public Health, Shandong University, Jinan 250012, China ; School of Public Health, Taishan Medical University, Taian 271016, China.

ABSTRACT
Citreoviridin (CIT), a mycotoxin produced by Penicillium citreonigrum, is a common contaminant of wide range of agriproducts and detrimental to human and animal health. In this study, the interaction of CIT with human serum albumin (HSA) is researched by steady-state fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD) methods, and molecular modeling. The association constants, binding site numbers, and corresponding thermodynamic parameters are used to investigate the quenching mechanism. The alternations of HSA secondary structure in the presence of CIT are demonstrated with UV-Vis, synchronous fluorescence, and CD spectra. The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via fluorescence resonance energy transfer method.

No MeSH data available.


Related in: MedlinePlus

UV absorption spectra of the CIT-HSA. The concentration of HSA was 1.5 μM while the CIT concentration corresponding to 0, 3.33, 6.67, 10, and 13.3 μM is from a to e, respectively. f [HSA] = 0 μM, [CIT] = 15.0 μM. Tris buffer, pH = 7.4, T = 297 K.
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fig4: UV absorption spectra of the CIT-HSA. The concentration of HSA was 1.5 μM while the CIT concentration corresponding to 0, 3.33, 6.67, 10, and 13.3 μM is from a to e, respectively. f [HSA] = 0 μM, [CIT] = 15.0 μM. Tris buffer, pH = 7.4, T = 297 K.

Mentions: Figure 4 shows the UV-Vis absorption spectra of HSA in the absence and presence of CIT. Three absorption peaks at 210, 277, and 367 nm are observed in Figure 4. The intensities of these peaks rise upon the addition of CIT. The absorption of HSA at 210 nm represents the content of α-helix in the protein [30]. The peak at 210 and 280 nm will be found to slightly shift towards shorter wavelengths with the increasing amounts of CIT, which indicate a decrease of α-helix and tryptophan (Trp) residue is exposed to a more hydrophobic environment.


Binding of citreoviridin to human serum albumin: multispectroscopic and molecular docking.

Hou H, Qu X, Li Y, Kong Y, Jia B, Yao X, Jiang B - Biomed Res Int (2015)

UV absorption spectra of the CIT-HSA. The concentration of HSA was 1.5 μM while the CIT concentration corresponding to 0, 3.33, 6.67, 10, and 13.3 μM is from a to e, respectively. f [HSA] = 0 μM, [CIT] = 15.0 μM. Tris buffer, pH = 7.4, T = 297 K.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4419221&req=5

fig4: UV absorption spectra of the CIT-HSA. The concentration of HSA was 1.5 μM while the CIT concentration corresponding to 0, 3.33, 6.67, 10, and 13.3 μM is from a to e, respectively. f [HSA] = 0 μM, [CIT] = 15.0 μM. Tris buffer, pH = 7.4, T = 297 K.
Mentions: Figure 4 shows the UV-Vis absorption spectra of HSA in the absence and presence of CIT. Three absorption peaks at 210, 277, and 367 nm are observed in Figure 4. The intensities of these peaks rise upon the addition of CIT. The absorption of HSA at 210 nm represents the content of α-helix in the protein [30]. The peak at 210 and 280 nm will be found to slightly shift towards shorter wavelengths with the increasing amounts of CIT, which indicate a decrease of α-helix and tryptophan (Trp) residue is exposed to a more hydrophobic environment.

Bottom Line: Citreoviridin (CIT), a mycotoxin produced by Penicillium citreonigrum, is a common contaminant of wide range of agriproducts and detrimental to human and animal health.The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with hydrophobic and hydrogen bond force.Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via fluorescence resonance energy transfer method.

View Article: PubMed Central - PubMed

Affiliation: School of Public Health, Shandong University, Jinan 250012, China ; School of Public Health, Taishan Medical University, Taian 271016, China.

ABSTRACT
Citreoviridin (CIT), a mycotoxin produced by Penicillium citreonigrum, is a common contaminant of wide range of agriproducts and detrimental to human and animal health. In this study, the interaction of CIT with human serum albumin (HSA) is researched by steady-state fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD) methods, and molecular modeling. The association constants, binding site numbers, and corresponding thermodynamic parameters are used to investigate the quenching mechanism. The alternations of HSA secondary structure in the presence of CIT are demonstrated with UV-Vis, synchronous fluorescence, and CD spectra. The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via fluorescence resonance energy transfer method.

No MeSH data available.


Related in: MedlinePlus