Abstract
Immunotherapy is one of the most recently used treatments for numerous cancer types and also some autoimmune and inflammatory diseases. One of the valuable targets for immunotherapy is Interleukin-17A (IL-17A) or its receptor (IL-17RA) because overexpression of IL-17A as a pro-inflammatory cytokine is associated with several inflammatory, autoimmune and cancer diseases. In this study, the extracellular domain of IL-17RA involved in binding to IL-17A was mutated by using R software to achieve a variant with increased binding affinity to IL-17A. The ∆∆G value of -30.89 kcal/mol was calculated for the best variant (385) with point mutations of R265N, N91T, and W31K using the FoldX module. Also, the KD for its interaction with IL-17A was calculated 0.06 nM by surface plasmon resonance (SPR) technique. Our results indicated that variant 385 could bind to IL-17A with higher binding affinity than wild-type one, so, it can be a good therapeutic candidate for blocking IL-17A.