| Literature DB >> 30917192 |
Jeffrey R Brender1, Anirban Ghosh, Samuel A Kotler, Janarthanan Krishnamoorthy, Swapna Bera, Vanessa Morris, Timir Baran Sil, Kanchan Garai, Bernd Reif, Anirban Bhunia, Ayyalusamy Ramamoorthy.
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.Entities:
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Year: 2019 PMID: 30917192 PMCID: PMC6544147 DOI: 10.1039/c9cc01067j
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222