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Insights into the molecular mechanism behind solubilization of amyloidogenic polyglutamine‐containing peptides
Author(s) -
Burra Gunasekhar,
Thakur Ashwani Kumar
Publication year - 2019
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24094
Subject(s) - monomer , trifluoroacetic acid , chemistry , solubilization , intramolecular force , solubility , mechanism (biology) , intermolecular force , combinatorial chemistry , peptide , protein folding , biochemistry , organic chemistry , molecule , polymer , philosophy , epistemology
Synthetic 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.