De novo design of a two-stranded coiled-coil switch peptide.

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 Biol

authors

Kammerer RA,Steinmetz MO

doi

10.1016/j.jsb.2006.01.017

subject

Has Abstract

pub_date

2006-08-01 00:00:00

pages

146-53

issue

2

eissn

1047-8477

issn

1095-8657

pii

S1047-8477(06)00103-1

journal_volume

155

pub_type

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