Chemotactic cytokines or chemokines are small signalling proteins responsible for the recruitment of leukocytes to sites of inflammation. Although, chemokines are critical to orchestrate effective immune response, many have been associated to several inflammatory disorders. Despite being recognised as therapeutic target, no efficient treatments targeting the chemokine network for inflammatory diseases are available to date. This is attributed with the complexity of the many and varied chemokine interactions with themselves, their receptors and glycosaminoglycans on extracellular matrix. Thus, the pharmaceutical industry dogma of "one molecule, one target" is rendered ineffective against this network. Evasins are small tick saliva proteins that can bind and neutralise several chemokines, therefore allowing the tick to feed on their host for days without sparking an immune response. The potential of Evasins as effective anti-inflammatory agents was proven in many pre-clinical disease models. The interest in Evasins led to the discovery of a novel Evasin, P672, that can bind a wide range of CC chemokines. This work describes the discovery of peptides inspired by the chemokine binding site of P672. These peptides were shown to neutralise several chemokines and exhibited in vivo anti-inflammatory activity. A novel generation of P672-inspired peptides were designed and exhibited multiple chemokine-binding properties with increased human plasma resistance. Finally, P672/chemokine interfaces were mapped using peptide display techniques informing on P672 binding sites and its mode of action to neutralise chemokines. This work demonstrates the exciting potential of utilising Evasin/chemokine interaction studies with informed mode of action as starting points for anti-inflammatory peptide development.