Premium
Kinetic and thermodynamic stability of bacterial intracellular aggregates
Author(s) -
Espargaró Alba,
Sabaté Raimon,
Ventura Salvador
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.09.049
Subject(s) - intracellular , protein aggregation , chemistry , biophysics , protein stability , solubility , peptide , in vivo , chemical stability , protein folding , biochemistry , biology , microbiology and biotechnology , organic chemistry
Protein aggregation is related to many human disorders and constitutes a major bottleneck in protein production. However, little is known about the conformational properties of in vivo formed aggregates and how they relate to the specific polypeptides embedded in them. Here, we show that the kinetic and thermodynamic stability of the inclusion bodies formed by the Aβ42 Alzheimer peptide and its Asp19 alloform differ significantly and correlate with their amyloidogenic propensity and solubility inside the cell. Our results indicate that the nature of the polypeptide chain determines the specific conformational properties of intracellular aggregates. This implies that different protein inclusions impose dissimilar challenges to the cellular quality‐control machinery.