Abstract
The interaction of clenbuterol hydrochloride (CL) to bovine hemoglobin (BHb) under physiological conditions was investigated by using UV-vis absorption, fluorescence, circular dichroism (CD) and molecular modeling. The fluorescence intensity of BHb decreased regularly with the gradual increasing concentration of CL. It is observed that there was a prominent interaction between CL and BHb. The fluorescence data revealed that the fluorescence quenching is a static process, and the thermodynamic parameters were calculated according to the Van't Hoff equation. The alternations of protein secondary structure in the presence of CL were determined by the evidence of CD. Molecular modeling study that corroborate our experimental results revealed that the binding mode of CL–BHb complex could be attributed to the hydrophobic interaction and hydrogen bonding, but electronic interaction cannot be excluded.
Highlights
Clenbuterol hydrochloride (CL) was once used to improve the percent conversion of feed and the percent content of meat
The absorption maximum of Soret band is decreased with the addition of CL, while the maximum absorption wavelength remains unchanged, which indicates that the heme is not exposed from the crevices at the exterior of the subunit and CL is integrated into the hydrophobic pocket of Bovine hemoglobin (BHb)
The result of UV/vis absorption measurement results showed that there was a permanent interaction between BHb and CL, and the fluorescence quenching was due to the formation of BHb–CL complex [7]
Summary
Clenbuterol hydrochloride (CL) was once used to improve the percent conversion of feed and the percent content of meat. It is one of synthetic β-adrenoceptor agonist, an amine derivative of phenylethyl alcohol, and the chemical name is 1-(4-amino-3, 5-dichlorophenyl)-2-tertbutylaminoethanol hydrochloride. Hemoglobin (Hb) is one of the most significant proteins in the blood plasma of higher organisms. Hb is well known for its function in the blood circulatory system that working as a transporter of oxygen. It carries and releases oxygen to the low oxygen partial pressure tissues through the blood circulatory [11]. Bovine hemoglobin (BHb) has a molecular weight of 64,500 and contains four globin chains, two identical α-chains of 141 amino acids each and two identical β-chains of 146 amino acid each [8]
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