Investigation on the interaction between angiotensin I converting enzyme inhibitory peptide to human hemoglobin by synchronous fluorescence technique in the absence and presence of electromagnetic fields

ACE inhibitors (Angiotensin converting enzyme) are a group of drugs used to treat high blood pressure. For the first time, the ACE enzyme inhibitors were extracted from Brazilian serum poison is called Bothrops Jararaca. The Teprotide has 9 amino acids that inhibites ACE and reduces blood pressure when administered intravenously. The interaction of drugs with hemoglobin is very important in that it is the most abundant protein in the blood, and most drugs will come into contact with this protein when entering and transfusion. The purpose of this study was to investigate the effects of low frequency electromagnetic fields on the interaction of human hemoglobin protein and ACE inhibitor peptide by synchronous fluorescence technique. Because low-frequency electromagnetic fields are used in certain pathological conditions for treatment. At the first time, Lloyd introduced the Synchronous fluorescence method in 1971. With the help of this method- in cases where several fluorophore samples are available- we are able to achieve a wider and more detailed information with minimum number of fluorescence intensities scanned. The Synchronous fluorescence emission spectrum was obtained in both the ∆λ=15 and ∆λ=60 wavelengths in the absence and presence of electromagnetic fields. The results indicate a decrease in fluorescence intensity in all cases, which shows a change in protein structure and the formation of a protein-peptide complex. At wavelength ∆λ=15, the emission maximum was observed to be shorter wavelengths, indicating a reduction in the polarity of the surrounding tyrosine environment. At wavelength ∆λ=60, the maximum emission did not pay attention that it is showed there was no change in polarity in the fluorophore environment. As observed, in Δλ = 15, the curve of the diagram in the presence of EMF at 100 KHz is higher indicating the stronger interaction between protein and peptide whereas in Δλ = 60, the curve of diagram in the absence of EMF is higher indicating stronger binding between Hb and peptide in the absence of EMF. As a result of the presence of electromagnetic field is caused to change the behavior of peptide and protein interactions.