Abstract
In this work, we monitor the alterations caused in membrane model systems upon the addition of biologically-relevant peptides. Our first study reports on the interaction with model membranes of an internal fusion peptide (SARSIFP) from the S2 subunit of the SARS coronavirus spike glycoprotein. It is believed that SARSIFP might be fundamental for the later steps of the fusion between the viral and host cellular membranes. Non-linear least-squares fits of stearic acid spin labels ESR spectra showed that the rotational dynamics of the HPS headgroup region and of the whole carbon chain of SDS surfactants was perturbed by the peptide.
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 callDisclaimer: 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.
