Abstract:
:The properties and characteristics shared by amyloid fibrils formed from disease and non-disease associated proteins that are unrelated in sequence and structure offer the prospect that model systems can be used to systematically assess the factors that predispose a native protein to form amyloid fibrils. Based on a de novo design approach, we recently reported a unique switch peptide model system, ccbeta, that forms a three-stranded coiled-coil structure at low temperatures and which can be easily converted to amyloid fibrils by increasing the temperature. To simplify the system further, we describe here the redesign of a two-stranded ccbeta coiled-coil variant and its detailed analysis by a variety of biophysical methods. Compared with the original design, the characteristics of the peptide make it even simpler to elucidate and validate fundamental principles of amyloid fibril-formation.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Kammerer RA,Steinmetz MOdoi
10.1016/j.jsb.2006.01.017subject
Has Abstractpub_date
2006-08-01 00:00:00pages
146-53issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(06)00103-1journal_volume
155pub_type
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