Abstract
Using NMR to probe transient binding of Aβ1-40 monomers to fibers, we find partially bound conformations with the highest degree of interaction near F19-K28 and a lesser degree of interaction near the C-terminus (L34-G37). This represents a shift away from the KLVFFA recognition sequence (residues 16-21) currently used for inhibitor design.
Originalsprache | Englisch |
---|---|
Seiten (von - bis) | 4483-4486 |
Seitenumfang | 4 |
Fachzeitschrift | Chemical Communications |
Jahrgang | 55 |
Ausgabenummer | 31 |
DOIs | |
Publikationsstatus | Veröffentlicht - 2019 |