Binding Analysis of Cholesterol and its Derivatives with 13 Chosen Respiratory Allergens: An In-silico Study

Background and Objectives

Respiratory allergens are generally non-parasite proteins in nature, which induces more amounts of Immunoglobulin E (Ig E) levels in atopic persons. A steady increasing prevalence of asthma and other allergy related disorders, which has been turn a huge public health issue throughout the globe. In the present investigation, we aimed to study four chosen cholesterol and its derivatives as potent modulating agents against 13 selected respiratory allergens using docking methods.

Materials and Methods

The 13 chosen respiratory allergens proteins were studied on the docking behaviour with four selected ligands namely i) cholesterol, ii) 17:1 cholesteryl ester, iii) cholesterol formate and iv) cholesterol palmitate by using the swissdock method. In addition to docking, physicochemical properties of 13 chosen allergens proteins were determined using ProtParam web server.

Results

With reference to physicochemical property analysis, three selected respiratory allergen proteins (Mite allergen Bio t5, Major allergen Can f 1 and Allergen Can f 1) have exhibited instability index value greater (^˃) than 40. The docking results revealed that Mite allergen Der f 21.0101 has exhibited the Highest Binding Energy [HBE] with all four target ligands [i) cholesterol (-8.18 kcal/mol); ii) 17:1 cholesteryl ester (-10.48 kcal/mol); iii) cholesterol formate (-8.41 kcal/mol) and iv) cholesterol palmitate (-9.63 kcal/mol)]. Interestingly, Allergen Can f 1 has exhibited amino acids interaction with three target ligands [cholesterol (Pro55); 17:1 cholesteryl ester (Lys131); and cholesterol palmitate (Tyr97)].

Conclusion

Thus, the present finding gives new knowledge about the four selected ligands (cholesterol and its derivatives) as potent modulating agents against 13 chosen respiratory allergens, which will aid in developing allergy mitigation strategies.