Publications by authors named "Maliheh Sadat Atri"

Article Synopsis
  • - Aflatoxins, particularly AFB1 and AFG1, are toxic chemicals linked to liver damage and cancer, primarily through contaminated food and feed exposure.
  • - This study investigated how AFB1 and AFG1 interact with bovine α-lactalbumin (ALA), a key protein in milk, using fluorescence spectroscopy and molecular modeling techniques.
  • - Findings indicate that both aflatoxins significantly quench ALA's fluorescence and bind through hydrophobic interactions and hydrogen bonds, with AFG1 showing a stronger binding affinity than AFB1.
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The influence of κ-carrageenan (KC) depolymerization using ultrasound on its interaction with β-lactoglobulin (BLG) was investigated by isothermal titration calorimetry (ITC), turbidity measurement, dynamic light scattering and zeta-potential analyses. Time and amplitude of the sonication had a direct effect on the viscosity depression, while the sonication temperature had an opposite effect. ITC measurements indicated that the sonication significantly decreased the affinity constant between KC and BLG.

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Propensity of two different silver nanoparticles (Ag-NPs) to bovine hemoglobin (BHb) was investigated by means of spectroscopic methods. We have combined spectrophotometric and calorimetric methods to show that there is no significant interaction between citrate-coated Ag-NPs and BHb at physiological pH and 20°C. However, our previous results show that polyethylene glycol-coated Ag-NPs strongly bind to Hb and effect on the secondary and tertiary structures of BHb.

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The stability of camel alpha-lactalbumin (alpha-la) against heat denaturation was measured, using circular dichroism (CD) and fluorescence spectroscopy, as well as differential scanning calorimetry (DSC). The experiments were performed in the presence of saturating concentrations of calcium as well as in the presence of EDTA, yielding to the apo form of alpha-la. The change in heat capacity (DeltaCp) suggests a greater contribution of hydrophobic interactions to the stability of holo camel alpha-la than in its bovine counterpart.

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