Intrinsically disordered presynaptic neuronal protein, α-Synuclein plays a critical role in synaptic vesicle trafficking, though the exact mechanism still remains unknown. It is also amyloidogenic in nature and deposits of higher aggregates of α-Synuclein in the Lewy bodies are the histopathological hallmark of second most prevalent neurodegenerative disorder, Parkinson’s disease. Posttranslational modifications α-synuclein such as ubiquitination, phosphorylation and nitrosylation, play a crucial role in modulation of α-synuclein aggregation kinetics. SUMOylation, a post-translational modification involving covalent attachment of SUMO to the target protein has been shown to abolish α-synuclein fibril formation. In our study, we showed that SUMO-1 interacts non-covalently with α-synuclein and alters the aggregation kinetics of α-Synuclein by using ThT fluorescence, circular dichroism, nuclear magnetic resonance spectroscopy and atomic force microscopy. Interaction with SUMO results in the delayed aggregation rate of α-Synuclein. The residues specific interaction studied by solution state NMR reveals that, SUMO1 interacts to the protein in the N-terminal region which has been previously shown to form a β-hairpin loop structure which upon sequestration completely inhibits α-Synuclein aggregation. This study gives a better insight about the SUMO and Synuclein interaction and may suggest a new signaling or regulatory mechanism of SUMO in Parkinson’s disease.