Chemokines are the central mediators of inflammatory cascade. The process is initiated by binding of chemokines to their receptors expressed on the surface of leukocytes, resulting their migration towards the site of the affected tissue. Evasins, the tick salivary proteins, bind to chemokines and prevent activation of receptor to subvert the host immune response. Apart from well characterised evasins: Evasin-1 and Evasin-4, we characterised and validated the chemokine binding ability of EVA-P974 from Amblyomma cajennense and EVA-RPU-02 from Rhipicephalus pulchellus. Our crystal structure of EVA-P974 complexed to two different chemokines (CCL7 and CCL17) with extensive mutational analysis, revealed the role of N-terminus in binding affinity and selectivity. This is further supported by the role of presence of amino acid residues that will be sulfated and enhanced binding profile with chemokines. We designed chimeric evasins by interchanging N-terminal regions between EVA-1, EVA-4, EVA-P974 and EVA-RPU802 and expressed, purified, and examined their chemokine binding properties. In line with our hypothesis, we found that the chemokine binding selectivity and affinity of chimeric evasins altered while exchanging N-terminal regions. The chimeric evasin consisting N-terminus of EVA-4 and core region of EVA-RPU802 appeared absolutely selective to CCL8 (KD 64.4 ± 0.08 nM). Likewise, another chimeric evasin which contains N-terminus of EVA-1 and core region of EVA-RPU802 was able to bind to CCL14 selectively. We found that different evasins achieve binding to similar group of chemokines by utilising different residues. Overall, our study showed that the chemokine binding specificity and affinity of evasins can be altered by interchanging the N-terminal region. This study also provides the proof of hypothesis that the evasins can be semi-rationally engineered by interchanging their N-terminal regions to alter the chemokine binding selectivity and affinity.