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Updated: Jun 15, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
Published on: August 20, 2018
Relation between serum amyloid A truncated peptides and their suprastructure chirality
Noa Rubin1, Emanuel Perugia, Sharon G Wolf
1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel 76100.
Amyloid fibers formed from serum amyloid A (SAA) peptides can exhibit distinct left-handed or right-handed suprastructural chirality. This switch, influenced by peptide sequence, alters molecular structure and FTIR spectra, impacting amyloid formation.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Amyloids are protein aggregates linked to over 20 diseases.
- Amyloid fibers feature a cross-beta motif with beta-strands perpendicular to the fiber axis.
- Existing models describe specific amyloid structures but lack comprehensive understanding of chirality's role.
Purpose of the Study:
- To investigate the correlation between suprastructural chirality, molecular structure, and molecular chirality in amyloids.
- To explore how truncated serum amyloid A (SAA) peptides with identical core sequences form different amyloid structures.
- To determine the impact of specific amino acid mutations on amyloid fiber chirality.
Main Methods:
- Synthesis and characterization of truncated serum amyloid A (SAA) peptides.
- Analysis of suprastructural chirality using techniques like X-ray diffraction (implied).
- Fourier-transform infrared (FTIR) spectroscopy to analyze molecular structure and hydrogen bonding.
Main Results:
- Truncated SAA peptides SAA(2-6), SAA(1-11), and most SAA(2-9) formed left-handed amyloid fibers, consistent with the beta-sheet protofilament model.
- SAA(1-12), SAA(2-12), and SAA(1-12) variants with C-terminal mutations formed right-handed helical amyloid fibers.
- Right-handed fibers showed a red-shifted amide I peak in FTIR spectra compared to left-handed fibers, indicating structural differences.
Conclusions:
- Short amyloidogenic peptide fragments can fold into distinct amyloid structures with different suprastructural chiralities.
- The C-terminal region and specific mutations significantly influence the helical handedness of SAA amyloid fibers.
- Amyloidogenic core sequences may adopt different structures when isolated compared to their role in full-length proteins.
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