Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer’s amyloid Aβ10–35 peptide in solution and in SDS micelles

Usachev, Konstantin S.; Филиппов, А. В.; Antzutkin, Oleg N.; Клочков, В. В.

doi:10.1007/s00249-013-0928-7

Cited by 13 publications

(4 citation statements)

References 32 publications

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“…One NMR study found Aβ 1–40 to adopt an 3 10 -helix in residues 13–23 in aqueous environment (PDB ID 2LFM) [19]. Another NMR study found Aβ 10–35 to adopt an α-helix in residues 13–23 and 30–35 inside SDS micelles [20]. However, at pH 7.3 Aβ 10–35 is unstructured and adopts a compact random-coil conformation.…”

Section: Discussionmentioning

confidence: 99%

“…Remarkably, one attempt to determine the NMR structure without TFE at physiological conditions, revealed Aβ to adopt a 3 10 -helical structure incongruent with previous α-helical observations [19]. Finally, another NMR study used micelles to determine the structure of Aβ 10–35 and found it to possess two α-helical regions within residues 13–23 and 30–35 [20]. …”

Section: Introductionmentioning

confidence: 99%

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NMR structure of the water soluble Aβ17–34 peptide

Fonar

Samson

2014

Bioscience Reports

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Alzheimer's disease is the most common neurodegenerative disorder in the world. Its most significant symptoms are memory loss and decrease in cognition. Alzheimer's disease is characterized by aggregation of two proteins in the brain namely Aβ (amyloid β) and tau. Recent evidence suggests that the interaction of soluble Aβ with nAChR (nicotinic acetylcholine receptors) contributes to disease progression. In this study, we determine the NMR structure of an Aβ17–34 peptide solubilized by the addition of two glutamic acids at each terminus. Our results indicate that the Aβ peptide adopts an α-helical structure for residues 19–26 and 28–33. The α-helical structure is broken around residues S26, N27 and K28, which form a kink in the helical conformation. This α-helix was not described earlier in an aqueous solution without organic solvents, and at physiological conditions (pH 7). These data are in agreement with Aβ adopting an α-helical conformation in the membrane before polymerizing into amyloid β-sheets and provide insight into the intermediate state of Aβ in Alzheimer's disease.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

NMR structure of the water soluble Aβ17–34 peptide

Fonar

Samson

2014

Bioscience Reports

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“…Several Aβ fragments react similarly to the parent peptides when placed in the SDS micelle system. In particular, different studies have been performed to investigate the behavior in SDS micelles of Aβ fragments encompassing residues 10 Y-M 35 [ 38 , 39 , 40 , 41 ]. Among these fragments, Aβ(25−35) represents the shortest sequence of Aβ able to mimic the biological behavior of the full-length amyloid peptides, forming large β-sheet aggregates and reproducing the toxicity of the peptide [ 21 , 42 , 43 , 44 , 45 ].…”

Section: Introductionmentioning

confidence: 99%

Monitoring the Conformational Changes of the Aβ(25−35) Peptide in SDS Micelles: A Matter of Time

Santoro

Buonocore

Grimaldi

et al. 2023

IJMS

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Alzheimer’s disease is a neurodegenerative disease characterized by the formation of amyloid plaques constituted prevalently by amyloid peptides. Due to the well-known challenges related to the study in solution of these peptides, several membrane-mimicking systems such as micelle constituted by detergent—i.e., DPC and SDS—have been deeply investigated. Additionally, the strategy of studying short fragments instead of the full-length peptide turned out to be advantageous in exploring the structural properties of the different moieties in Aβ in order to reproduce its pathologic effects. Several studies reveal that among Aβ fragments, Aβ(25−35) is the shortest fragment able to reproduce the aggregation process. To enrich the structural data currently available, in the present work we decided to evaluate the conformational changes adopted by Aβ(25−35) in SDS combining CD and NMR spectroscopies at different times. From the solved structures, it emerges that Aβ(25−35) passes from an unordered conformation at the time of the constitution of the system to a more ordered and energetically favorable secondary structure at day 7, which is kept for 2 weeks. These preliminary data suggest that a relatively long time affects the kinetic in the aggregation process of Aβ(25−35) in a micellar system, favoring the stabilization and the formation of a soluble helix conformation.

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“…Nevertheless, interactions of different drugs with phospholipid aggregates can be effectively studied by NMR using model membranes. One of the commonly used membrane models in NMR work is the sodium dodecyl sulfate (SDS) micelle . The detergent head groups of SDS may be designed to physically mimic the surface of a biological membrane.…”

Section: Introductionmentioning

confidence: 99%

Structure of pravastatin and its complex with sodium dodecyl sulfate micelles studied by NMR spectroscopy

Galiullina

Rakhmatullin

Klochkova

et al. 2014

Magnetic Reson in Chemistry

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The aim of this work was to study the mechanisms of interaction between pravastatin and cell membranes using model membranes (sodium dodecyl sulfate micelles) by nuclear magnetic resonance spectroscopy methods. On the basis of the nuclear magnetic resonance experiments, it was established that pravastatin can form intermolecular complexes with sodium dodecyl sulfate micelles by the interaction of its hydrophilic groups with the polar surface of the micelle. Conformational features of pravastatin molecule were also studied.

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Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer’s amyloid Aβ10–35 peptide in solution and in SDS micelles

Cited by 13 publications

References 32 publications

NMR structure of the water soluble Aβ17–34 peptide

NMR structure of the water soluble Aβ17–34 peptide

Monitoring the Conformational Changes of the Aβ(25−35) Peptide in SDS Micelles: A Matter of Time

Structure of pravastatin and its complex with sodium dodecyl sulfate micelles studied by NMR spectroscopy

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