Prediction of Physicochemical Properties, Antioxidant Activity, and Transmembrane Helices of Alpha and Beta Globin Chains of Hemoglobin

Background: This study aimed to predict the physicochemical properties, antioxidant activity, and potential penetration of alpha helices of the alpha- and beta-globin chains of human hemoglobin in membranes of red blood cells (RBCs). Methods: The physicochemical properties of hemoglobin's alpha- and beta-globin chains were predicted using the ProtScale tool. Antioxidant activity was predicted using AnOxPePred, and transmembrane regions were identified using TMHMM‑۲.۰. Statistical analysis was conducted using the Kolmogorov-Smirnov test and Pearson correlation in SPSS software (version ۲۷). Results: Based on the prediction results, a significant direct correlation was observed between hydrophobicity and membrane‑anchoring tendency for both alpha globin (r = ۰.۴۹۴, P < ۰.۰۰۱) and beta-globin (r = ۰.۸۶۹, P < ۰.۰۰۱) chains. The highest free radical scavenging (FRS) score in the alpha globin chain was associated with the sequence WGKVGAHAGEYGAEALERMF (residues ۱۴-۳۳), while the highest FRS in the beta-globin chain was linked to the sequence VLVCVLAHHFGKEFTPPV (residues ۱۱۳-۱۲۶). Alpha globin chains showed a higher tendency to penetrate the inner layer of the cell membrane of red blood cells (RBCs) than beta-globin chains. Discussion: The study predicted that high FRS scores are located on the outer surface of alpha- and beta-globin chains, particularly at loop structures and junctions. Alpha globin chains are more likely to penetrate the cell membrane. Conclusion: Regions with higher FRS scores are more exposed to the cytoplasm, which contains more free radicals.

کلیدواژه ها:

Hemoglobin ، Antioxidant ، Transmembrane Alpha Helices ، Antioxidant Activity ، Physicochemical Properties