Alzheimer's disease (AD) is one of the most significant social and health burdens of the present century. Plaques formed by extracellular deposits of amyloid (A) are the prime player of AD's neuropathology. Studies have implicated the varied role of phospholipase A(2) (PLA(2)) in brain where it contributes to neuronal growth and inflammatory response. Overall contour and chemical nature of the substrate-binding channel in the low molecular weight PLA(2)s are similar. This study involves the reductionist fragment-based approach to understand the structure adopted by N-terminal fragment of Alzheimer's A peptide in its complex with PLA(2). In the current communication, we report the structure determined by X-ray crystallography of N-terminal sequence Asp-Ala-Glu-Phe-Arg-His-Asp-Ser (DAEFRHDS) of A-peptide with a Group I PLA(2) purified from venom of Andaman Cobra sub-species Naja naja sagittifera at 2.0 angstrom resolution (Protein Data Bank (PDB) Code: 3JQ5). This is probably the first attempt to structurally establish interaction between amyloid- peptide fragment and hydrophobic substrate binding site of PLA(2) involving H bond and van der Waals interactions. We speculate that higher affinity between A and PLA(2) has the therapeutic potential of decreasing the A-A interaction, thereby reducing the amyloid aggregation and plaque formation in AD.