The self-assembly properties of all possible stereoisomers of terminally protected Boc-Val-Phe-Phe-OMe, having sequence homogeneity with Alzheimer's amyloidbeta (Aβ 18-20 ) peptide was investigated. The morphology analysis by field emission scanning microscope (FE-SEM) revealed that protected VFF and vff (small letters denote one letter code of D-amino acids) exhibited a ribbon-like fibrous network, vFF, Vff, VfF, and vFf formed rod-like structures. Although VFf exhibited a mixture of two morphologies (rod-like and spherical), vfF showed spherical structures predominantly. The single-crystal X-ray diffraction (SC-XRD) indicated that five of the stereoisomers formed a parallel beta-sheet arrangement. In higher-order packing, while Vff, VfF, and vFf exhibited supramolecular sheet-like architecture, VFf and vfF pair showed helical sheet-like arrangement. All corresponding enantiomers displayed identical morphology but opposite conformation. The chirality of amino acids in peptides played a significant role in their supramolecular arrangements. Interestingly, all self-aggregated peptides can bind with amyloid binding dye thioflavin T.