Helicobacter pylori (H. pylori) is able to colonize the human stomach. It possesses urease on its surface and this degrades urea to generate ammonia, which neutralizes the bacterial environment. H. pylori infection is a public concern because of its wide prevalence, pathogenicity and carcinogenicity. Recent research has revealed that H. pylori urease also acts as an adhesin to assist in adhesion of bacteria to gastric mucosa. Because adhesion is a pivotal step in chronic infection, substances that inhibit adhesion have been investigated. Through a series of studies, we developed a conjugated caseinate, FP-10, derived from milk protein that is able to effectively inhibit the adhesion of H. pylori to gastric mucosa. Its efficacy has been confirmed in vitro and in vivo, in both animal studies and clinical trials. This review summarizes the studies concerning the adhesion mechanism and development of FP-10.