Microtubular structures were self-assembled in aqueous media from a newly synthesized bolaamphiphile, bis(N--amido-threonine)-1,3-propane dicarboxylate. The self-assembly process was examined at varying pH. The formed microtubes were then functionalized with the highly glycosylated protein mucin. In nature, the O-linked saccharides of mucin are generally associated with Thr or Ser residues of protein scaffolds. In this work, peptide microtubes with threonine functionality were prepared synthetically in order to enhance the affinity of the microtubes toward mucin, thus mimicking natural proteins. After binding the mucin to the microtubes, we investigated the biocompatibility of those materials by conducting in vitro cell attachment, cell proliferation, and cytotoxicity studies using normal rat kidney (NRK) cells. The studies revealed that the biomaterials were nontoxic, biocompatible, and showed significant adhesion to the cells. It is well known that natural mucins may degrade into their motifs; however, upon binding to the surface of microtubes, their stability may be increased. Because mucin is one of the major components of mucoadhesion, and various types of mucins are ubiquitous in human tissues, such mucin-bound microtubes may potentially be used as mucoadhesive materials for targeted drug delivery and improve the localization of drugs.