Title

Towards the design of anti-amyloid short peptide helices

Authors

Irena Roterman^1*, Mateusz Banach¹, Leszek Konieczny²

Affiliation

¹Department of Bioinformatics and Telemedicine, Jagiellonian University–Medical College, Łazarza 16, 31-530 Krakow, Poland;
²Chair of Medical Biochemistry, Jagiellonian University–Medical College, Kopernika 7, 31-034
Krakow, Poland;

E-mail

mbkoniec@cyf-kr.edu.pl; myroterm@cyf-kr.edu.pl

Article Type

Hypothesis

Date

Received January 10, 2018; Revised January 25, 2018; Accepted January 25, 2018; Published January 31, 2018

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 terminal portion of the fibril). The emergence and elongation of fibrillary forms resulting from linear propagation of local hydrophobicity peaks is shown using the fuzzy oil drop model.

Keywords:

Amyloid; drug design; hydrophobicity.

Citation

Roterman et al. Bioinformation 14(1): 001-007 (2018)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.