α-Amino Acids were used as bridges to construct side chain-stapled analogs library of an IL-17A-binding peptide (HAP) and evaluated the staples chirality (L/D) impacts on the peptide‘s properties. While all AA-derived peptidyl staples drastically increase the enzymatic stability of HAP, the L-AA-based staples generate more significant impacts in increasing the helicity and binding affinity of the modified peptide compared to the D-amino acid bridges.