IL-6 is an important interleukin associated with inflammation and several diseases such as cancer. Evaluation of its levels in human blood sera is a critical step for an accurate diagnosis of the diseases. Our goal is to design peptides that can selectively bind in different poses with good affinities to IL-6. For this purpose, we started from the crystal structures of different IL-6/protein complexes available in the Protein Data Bank (PDB) to select short peptides in the interaction zones, in which we intentionally introduced point mutations to increase their stability and affinity. To examine their usefulness as capture and reporting probes for the IL-6 biosensing, the five peptides and their interaction with IL-6 were studied in saline aqueous solution. Molecular docking, MD, and MM-PBSA were used to investigate the affinity and stability of these complexes. The conformational changes, the distance between the mass centers, the gyration radii, and the numbers of hydrogen bonds were analyzed to select the most suitable candidates. Three peptides, namely CTE17, CAY15 and CSE25, have the highest affinities presenting significant numbers of residues that have contact frequencies greater than 50% of simulation run time and are the most promising candidates. CTE17 and CSE25 showed they can form a stable sandwich with the target protein. For sake of comparison, we examined the previously known peptides (FND20, INL19 and CEK17) having affinity to IL-6 and the affinity of the lead i.e. CSE25 to two other interleukin family members (IL-4 and to IL-10).