AI Article Synopsis
- The study utilizes NMR to investigate how Aβ1-40 monomers bind transiently to fibers.
- It identifies that the strongest interactions occur near specific residue pairs (F19-K28) and weaker interactions near the C-terminus (L34-G37).
- These findings suggest a need to rethink inhibitor designs by moving away from the previously focused KLVFFA sequence (residues 16-21).
Article 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.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6544147 | PMC |
| http://dx.doi.org/10.1039/c9cc01067j | DOI Listing |
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