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Comment
. 2013 Jul 16;105(2):287-8.
doi: 10.1016/j.bpj.2013.05.004.

Structural characterization and inhibition of toxic amyloid-β oligomeric intermediates

Ayyalusamy Ramamoorthy  1 , Mi Hee Lim
Affiliations
Comment

Structural characterization and inhibition of toxic amyloid-β oligomeric intermediates

Ayyalusamy Ramamoorthy et al. Biophys J. .
No abstract available

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Figures

Figure 1
Figure 1
(A) A partially folded structure of Aβ1-40 (PDB:2LFM) in solution determined by NMR spectroscopy (4). (B) NMR investigations for identification of interactions of Aβ with proteins, metal ions, and/or small molecules (6–9).
See this image and copyright information in PMC

Comment on

  • Aβ association inhibition by transferrin.
    Raditsis AV, Milojevic J, Melacini G. Raditsis AV, et al. Biophys J. 2013 Jul 16;105(2):473-80. doi: 10.1016/j.bpj.2013.03.065. Biophys J. 2013. PMID: 23870268 Free PMC article.

References

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    1. Raditsis A.V., Milojevic J., Melacini G. Understanding the molecular basis for the inhibition of the Alzheimer's Aβ-peptide oligomerization by transferrin using saturation transfer difference and off-resonance relaxation NMR spectroscopy. Biophys. J. 2013;105:473–480.
    1. Milojevic J., Melacini G. Stoichiometry and affinity of the human serum albumin-Alzheimer’s Aβ peptide interactions. Biophys. J. 2011;100:183–192. - PMC - PubMed
    1. Vivekanandan S., Brender J.R., Ramamoorthy A. A partially folded structure of amyloid-β (1–40) in an aqueous environment. Biochem. Biophys. Res. Commun. 2011;411:312–316. - PMC - PubMed
    1. Fezoui Y., Teplow D.B. Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization. J. Biol. Chem. 2002;277:36948–36954. - PubMed

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