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Possible targets for medical intervention include G\u2010quadruplexes (G4Qs) and their protein interaction partners. We investigated the stability and conformational space of the RG\u20101 RNA\u2010G\u2010quadruplex of the SARS\u2010CoV\u20102 N\u2010gene in the presence of salts, cosolutes, crowders and intrinsically disordered peptides, focusing on \u03b1\u2010Synuclein and the human islet amyloid polypeptide, which are involved in Parkinson's disease (PD) and type\u2010II diabetes mellitus (T2DM), respectively. We found that the conformational dynamics of the RG\u20101 G4Q is strongly affected by the various solution conditions. Further, the amyloidogenic peptides were found to strongly modulate the conformational equilibrium of the RG\u20101. Considerable changes are observed with respect to their interaction with human telomeric G4Qs, which adopt different topologies. These results may therefore shed more light on the relationship between PD as well as T2DM and the SARS\u2010CoV\u20102 disease and their molecular underpinnings. 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