Evaluation of the interaction between hemoglobin protein and angiotensin-inhibitory peptide by three-dimensional fluorescence method in the absence and presence of low-frequency electromagnetic fields

Farzaneh Sadeghzadeh,1,* Jamshidkhan chamani1*,2 Farzin hadizadeh2,3



Million people in worldwide are suffering from high blood pressure and related diseases. over the past two decades, there has been a dramatic increase in scientific knowledge and commercial production of bioactive peptides. these peptides in the cardiovascular system are known as anti-clotting compounds, antioxidant, cholesterol-lowering and anti-hypertensive agents. the angiotensin converting enzyme plays an important role in regulating blood pressure in the renin-angiotensin system. in this research, the anti-hypertensive activity of peptides extracted from egg whites was investigated. for this purpose, three-dimensional fluorescence method was used.


Hb with molecular mass of 64500 dalton, angiotensin i converting enzyme inhibitory peptide with molecular mass of 1582.74 dalton, phosphate potassium buffer. three-dimensional fluorescence is able to provide information on the protein structure for investigating the interaction of the angiotensin converting enzyme inhibitors peptide with the human hemoglobin protein and the effect of the peptide on the protein structure, as well as its variation in the presence of various electromagnetic fields and what effects of electromagnetic fields will have on protein-ligand interactions.


The results showed that the interaction between the human hemoglobin protein and the peptide occurred, followed by a change in the second structure and conformation of the protein.


: in the presence of emf of various changes in protein structure is observed.


Human hemoglobin, angiotensin i converting enzyme inhibitory peptide, three-dimensional fluorescence