Abstract
Monolayers of an amyloid β peptide (Aβ40) and a much smaller model peptide (LSFD) at the air/water interface have been investigated by isotherm, IRRAS and GIXD measurements. Additionally, the LSFD monolayer has been transferred onto solid support and investigated by ATR–FTIR to test the influence of the transfer on the secondary structure of the peptide. Both peptides are surface active and form stable films of ordered β-sheet domains on the surface. The same absorption bands characteristic of an anti-parallel β-sheet conformation can be seen in the transferred LSFD film indicating that the transfer does not change the secondary structure. On the water surface, the β-sheets are oriented mostly parallel to the surface. GIXD experiments show a Bragg peak at characteristic repeat distances of 4.75–4.8 Å for both peptides. The full-width at half maximum (fwhm) of this peak shows that the smaller LSFD peptide forms a monolayer film with high degree of order perpendicular to the β-strands, whereas Aβ40 exhibits a drastically reduced crystallinity.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Colloids and Surfaces A: Physicochemical and Engineering Aspects
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
