Towards the design of anti-amyloid short peptide helices.
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ABSTRACT:
SUBMITTER: Roterman I
PROVIDER: S-EPMC5818643 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
Publications
Towards the design of anti-amyloid short peptide helices.
Roterman Irena I Banach Mateusz M Konieczny Leszek L
Bioinformation 20180131 1
A set of short peptide sequences susceptible to fibrillar aggregation produces sequneces capable of arresting elongation of amyloid fibrils. The "stop" signals are short helices customized for each individual target. Such a helix should exhibit high amphiphilicity, with differing conditions present on each side (one side should be highly hydrophilic to enable water to interact with the aggregate, while the other side must retain a local distribution of hydrophobicity which matches that of the te ...[more]
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