Biomolecular peptides that can induce controlled interactions at the biomaterial interface while having a high affinity to the implant material provide a novel method to immobilize exosomes onto the Ti surfaces. Recently, Ti-binding peptides that electrostatically interacts with the amphoteric surface of Ti was isolate by peptide phage display methodology. In particular, minTBP-1, R(Arg)K(Lys)L(Leu)P(Pro)D(Asp)A(Ala), is a typical Ti-binding peptide that could specifically bind to Ti surfaces as follows: electrostatic interactions between –O− and –OH2+ groups from oxide films and R(Arg) and D(Asp) have been proposed to underlie the interaction between Ti surfaces and minTBP-1. Consequently, to functionalize Ti surfaces with exosomes, minTBP-1 and CP05 could be linked to construct chimeric peptide which maintain functions of both binding to Ti surface and capture exosomes.