Self-assembly of molecular building blocks is a ubiquitous process in biology. Here we focus on protein-inspired small self-assembling peptides. Proteins commonly function as homo-oligomers, with such complexes readily associating and dissociating in reponse to a biological trigger. Such subtle equilibria rely on protein-protein interfaces, which are evolutionary fine tuned and provide the necessary structural versitality though complementary non-covalent close contacts. We designed short peptide motifs of 7-8 residues from the β-continuous interface (two identical β-strands in anti-parallel close contact) of non-related homo-oligomeric proteins. The peptides sequences intrinsically self-assembled into nanostructrues with extended mophlogy in water, while retaining some property of the parent protein interface, espacially reversibility of assembly. All peptides at higher concentration in solution formed bifringent hydrogels with liquid crystalline textures observed for atleast three of them (Valery, Pandey et al. 2013). The results reveal a novel source of native self-assembling peptides. Insight into the self-assembly process of these peptide motifs will help better understand the hierarchial assembly in proteins and could also serve as a new system to be investigated for potential bionanotechnology applications, such as peptide based templates for fabricating conducting nanodevices.