Premium
Cover image
Publication year - 2019
Publication title -
peptide science
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24118
Subject(s) - monomer , chemistry , peptide , amyloid (mycology) , computer science , cover (algebra) , computational biology , biophysics , crystallography , biochemistry , biology , polymer , organic chemistry , inorganic chemistry , mechanical engineering , engineering
Protein aggregation into amyloid structures has been seen in numerous neurodegenerative diseases. To understand the misfolding and aggregation of these proteins, synthetic peptides are frequently studied; requiring monomeric solutions of aggregation‐prone peptides that are often insoluble. Burra and Thakur explore possible mechanisms behind the solubilization of polyglutamine peptides. The presence of intra‐ and/or inter‐molecular H‐bond networks renders the amorphous aggregates insoluble. During disaggregation, the H‐bonds are broken by the solvent, converting the peptides to either random coiled or α‐helical monomers, depending on the solvent used. Under physiological conditions, the monomers transform into ordered β‐strand rich amyloid‐like structures. (doi: 10.1002/pep2.24094 )