Based on a large spectrum of US28, planning to find out new antagon. Membrane spanning domain and epitopes were used to predict a binding mimotope that US28 bound with CC chemokines, the result of which were used to design and synthesize the peptide. The 12 peptide phage library was built sourcing from 25 different chemokines random phages including four families. The binding mimotope of synthesized peptide was screened by phage display technique, and assessed by ELISA assay. PL+S method was used to screen the 12 phage library with the target as biotinylated soluble form peptide H22. Biological activity of H22 were measured with cellular chemotaxis assays and calcium mobilization. Amino acid sequences of the displayed peptides in 10 phage clones were deduced from DNA sequences. They are GSESLNAHCALW, EIDGFNAHCALL, VIARLNAHCALR, ATECLNAHCALW, VIESLNAHCALW, DNGSINAHCALL and VKKTLNAHCALR. Every peptide sequence contains at least 2 hydrophobic residues. Eight of the 10 clones have a conservative sequence LNAHCAL. Chemotaxis assays showed that H22 induced migration of peripheral blood mononuclear, and H22 suppressed PBMCs' migration induced by hMIP-1β and EC₅₀=30.9 μg/L. H22 itself was not remarkably associated with the normal, rapid mobilization of calcium from intracellular stores. Instead, it blocked calcium mobilization induced by endogenous chemokines. It proves that using chemokine sequence of human source to build a peptide library and screen effective sequence is available. The conservative sequence could simulate the binding mimotope of Human MIP-1β interacting with HCMV US28 N-terminus to bind with synthesized peptide H22. The study has demonstrated that peptide H22 cannot stop the biological function of hMIP-1β and block the signal transduction from hMIP-1β by the way of calcium pathway, but itself did not affect cells activity.