The exploration of the potentials of peptide in drug delivery has led to numerous studies in peptide synthesis involving different protocols depending on the expected final products. In this study, we explored the self-assembling behavior of sulfanilic acid by reacting it with two hydrophobic amino acids namely valine and alanine using the linear polypeptide synthesis protocol. The reaction consequently resulted in bonding together of linear fibrous structures. Results on scanning electron microscope revealed that the individual fibers separated upon the introduction of aniline, an increased length and further observation showing that the fibers were altered into four different structures. Results on X-ray diffraction revealed that amide C-N bond in a peptide was found to be shorter than the C-N bond in a simple amine and residue backbone dihedral angles of around −60° and −45° in α-helix formation, while the dramatic rotation around the N2_C2_ bond resulted in tube. On the other hand, results on atomic force microscopy (AFM) revealed a fairly rough surface, while differential scanning calorimeter (DSC) results indicated that, at Tg (85 °C), the fibers underwent endothermic decomposition of about −2.5 mg and experienced an exothermic recrystallization at 125 °C. Results on thermogravimetric analysis (TGA) confirmed that the fiber was stable at 180 °C.