SDS Can Be Utilized as an Amyloid Inducer: A Case Study on Diverse Proteins

Khan, Javed Masood; Qadeer, Atiyatul; Chaturvedi, Sumit Kumar; Ahmad, Ejaz; Rehman, S.A. Abdul; Gourinath, S.; Khan, Rizwan Hasan

doi:10.1371/journal.pone.0029694

Cited by 116 publications

(59 citation statements)

References 27 publications

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“…Therefore, the structural state with the highest ␤-structure content is the most aggregation-prone state as demonstrated by ThT fluorescence experiments. SDS generally induces amyloid formation within a relatively narrow submicellar concentration range (17,19,64). Transient interactions between free peptide and surfactant-A␤ co-aggregates may mediate the conformational transition, although, at any given time point, only a small population that undergoes dynamic exchange is bound to the co-aggregates.…”

Section: Discussionmentioning

confidence: 99%

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Abelein

Kaspersen²,

Nielsen

et al. 2013

Journal of Biological Chemistry

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Background: ␤-Structured oligomers of the amyloid ␤ peptide are considered neurotoxic and on-pathway to amyloid fibril formation. Results: Surfactant-induced co-aggregated oligomers show dynamic rapid exchange with free peptide during a slow fibril formation process. Conclusion: ␤-Structure inducing small molecules kinetically promote peptide assembly into co-aggregates. Significance: Knowledge about molecular mechanisms of peptide aggregation modulators is potentially helpful for therapeutic purposes.

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Section: Discussionmentioning

confidence: 99%

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Abelein

Kaspersen²,

Nielsen

et al. 2013

Journal of Biological Chemistry

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“…4B), so that by 12 h, the CD spectrum still showed a complex of b-sheet and random coil structures, as indicated by two broad negative minima around 203 and 225 nm, consistent with previous studies. 68,69 This conformational stabilization effect could also be reected in the inhibitory effect of brazilin. Until 48 h, a CD spectrogram of corresponding to b-sheet conformation was observed in the presence of brazilin, although the values of the peak and valley had slightly changed compared with pure hIAPP.…”

Section: Effects Of Brazilin On the Secondary Structure Of Hiappmentioning

confidence: 99%

Brazilin inhibits fibrillogenesis of human islet amyloid polypeptide, disassembles mature fibrils, and alleviates cytotoxicity

Guo

Sun

et al. 2017

RSC Adv.

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Fibrillogenesis of human islet amyloid polypeptide (hIAPP) is a pathological hallmark of type II diabetes mellitus (T2DM), and the inhibition of hIAPP fibrillogenesis is an important strategy for the prevention and treatment of T2DM. In this study, the inhibitory effects of brazilin on the fibrillization and cytotoxicity of hIAPP were examined using the thioflavin T fluorescence (ThT) assay, transmission electron microscopy (TEM), circular dichroism (CD) spectroscopy, cytotoxicity assays, and molecular dynamics simulations.Both the ThT and TEM results have shown that brazilin inhibits hIAPP fibrillogenesis in a dose-dependent manner. CD studies revealed that brazilin delays the conformational transition of hIAPP from its initial ahelical to the b-sheet form. As a result, brazilin greatly alleviates hIAPP-induced cytotoxicity. Moreover, we also found that brazilin disassembles preexisting hIAPP fibrils, and alleviates the cytotoxicity of hIAPP aggregates. The results of free energy decomposition studies calculated using molecular mechanicsPoisson-Boltzmann surface area analysis revealed that hydrophobic interactions contribute more than 75% of the free energy of binding in the brazilin-hIAPP complex, while electrostatic interactions (i.e., hydrogen bonds) play a secondary role (<25%). Two binding sites of brazilin on the hIAPP pentamer were identified, encompassing the N-terminal region and the turn region. There are 11 important residues of hIAPP that strongly interact with brazilin -Asn3, Thr4, Thr9, Arg11, Asn14, Phe15, His18, Ser19, Ser20, Asn21 and Phe23. The findings presented here will contribute to a comprehensive understanding of the inhibitory effect of brazilin on the fibrillogenesis of hIAPP, which is critical for the search for more effective agents that can inhibit hIAPP fibrillogenesis.

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“…These studies were performed as previously described with modifications [31,32]. BSA (30 lM) in 50 mM sodium phosphate buffer at pH 7.0 was incubated at 70°C for 2.5 h with gentle agitation.…”

Section: Thioflavin T and Rayleigh Scattering Experimentsmentioning

confidence: 99%

Albumin-induced circular dichroism in Congo red: Applications for studies of amyloid-like fibril aggregates and binding sites

Vasconcelos

Ximenes

2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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SDS Can Be Utilized as an Amyloid Inducer: A Case Study on Diverse Proteins

Cited by 116 publications

References 27 publications

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Brazilin inhibits fibrillogenesis of human islet amyloid polypeptide, disassembles mature fibrils, and alleviates cytotoxicity

Albumin-induced circular dichroism in Congo red: Applications for studies of amyloid-like fibril aggregates and binding sites

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