Abstract
AbstractSynthetic peptides are widely used to understand the protein misfolding and aggregation observed in a diverse group of diseases called systemic amyloidosis and neurodegenerative disorders. The preparation of monomeric solutions of the aggregation‐prone peptides is necessary for achieving a mechanistic understanding efficiently, without compromising any critical step. This study describes novel approaches and mechanisms behind the conversion of otherwise insoluble/sparingly soluble peptides to soluble monomers by trifluoroacetic acid and hexafluoroisopropanol. Although the pretreatment with these solvents results in more or less similar monomers, the mechanism followed to achieve this differs with the solvent. Data show that these solvents aid in the solubility by disrupting the extensive intramolecular and/or intermolecular H‐bond network present in the insoluble peptides.
Published Version
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