Abstract:
:Investigation of the molecular mechanisms underlying amyloid-related human diseases attracts close attention. These diseases, the number of which currently is above 40, are characterized by formation of peptide or protein aggregates containing a cross-β structure. Most of the amyloidogenesis mechanisms described so far are based on experimental studies of aggregation of short peptides, intrinsically disordered proteins, or proteins under denaturing conditions, and studies of amyloid aggregate formations by structured globular proteins under conditions close to physiological ones are still in the initial stage. We investigated the effect of amino acid substitutions on propensity of the completely helical protein sperm whale apomyoglobin (sw ApoMb) for amyloid formation from its structured state in the absence of denaturing agents. Stability and aggregation of mutated sw ApoMb were studied using circular dichroism, Fourier transform infrared spectroscopy, x-ray diffraction, native electrophoresis, and electron microscopy techniques. Here, we demonstrate that stability of the protein native state determines both protein aggregation propensity and structural peculiarities of formed aggregates. Specifically, structurally stable mutants show low aggregation propensity and moderately destabilized sw ApoMb variants form amyloids, whereas their strongly destabilized mutants form both amyloids and nonamyloid aggregates.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Katina NS,Balobanov VA,Ilyina NB,Vasiliev VD,Marchenkov VV,Glukhov AS,Nikulin AD,Bychkova VEdoi
10.1016/j.bpj.2017.07.011subject
Has Abstractpub_date
2017-09-05 00:00:00pages
991-1001issue
5eissn
0006-3495issn
1542-0086pii
S0006-3495(17)30809-3journal_volume
113pub_type
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