In this paper we demonstrate that the mechanical performance of bacterial cellulose biomaterials can be enhanced by binding cellulose strands with monomeric alanine or glycine. Our inspiration for using these amino acids in monomeric form comes from a molecular dynamics comparison of flagelliform silk against its predominating amino acid components as bacterial cellulose bio-glues. Separate amino acids can be as good as flagelliform silk proteins for binding bacterial cellulose, since they have smaller sizes and are considerably more mobile. This is however not true of proline, which is present in flagelliform silk in similar amounts to alanine. This is because the attractive interactions of proline to bacterial cellulose are blocked somewhat by the presence of its rigid ring structure, which also limits mobility and flexibility in the molecule.