Amyotrophic lateral sclerosis (ALS) and Frontotemporal dementia (FTD) are caused by abnormal expansion of hexanucleotide repeats (HRE) GGGGCC (G4C2)n in a non coding region of the C9orf72 gene. Guanine-rich nucleic acid sequences can spontaneously assemble into G-quadruplexes and challenge the replication, transcription, and translation machinery. ALS and FTD linked GGGGCC-repeat containing DNA oligonucleotide folds into two distinct G-quadruplexes. Recently, the structural and topological diversity of G-quadruplexes have attracted great attention. The characterization of G-quadruplexes and understanding the mechanism of their folding/unfolding will help to design potential small molecules to target it. Herein, we describe the topology of (G4C2)8 G-quadruplex structure and influence of folding in the presence of myoinositol which is a carboxylic sugar abundant in brain. Circular dichrosium spectroscopy was employed to study the change in the properties and configurations of (G4C2)8 in the presence of myoinositol. The parallel topology of (G4C2)8 were observed in higher concentrations of myinositol osmolyte. The transition in the topology of (G4C2)8 was recored from anti-parallel to hybrid to parallel as the temperature and concentrations of myinositol were increased. At high temperature even low concentration of myinositol favour the parallel topology. Myoinositol was playing significant role in stabilizing the structures of (G4C2)8 and allow to adopt the parallel topology. Our findings are important in order to undertand the different folding of (G4C2)n and provided new insights about configurations of G-quadruplex which may use to design small molecules targing neurological disorders. Keywords- Folding/Unfolding, Guanine-Rich Nucleic Acid Sequences, Myoinositol, Neurological Disorders.