Influence of a curcumin derivative on hIAPP aggregation in the absence and presence of lipid membranes

Pithadia, Amit S.; Bhunia, Anirban; Sribalan, Rajendran; Padmini, Vediappen; Fierke, Carol A.; Ramamoorthy, Ayyalusamy

doi:10.1039/c5cc07792c

Cited by 67 publications

(44 citation statements)

References 40 publications

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“…To overcome this problem, several modified curcumin were synthesized for better solubility . Pithadia et al introduced the sodium acetate unit in curcumin C3 (Figure ) which improved water solubility as well as Human islet amyloid polypeptide aggregation activity …”

Section: Introductionmentioning

confidence: 99%

“…[21,22] Pithadia et al introduced the sodium acetate unit in curcumin C3 ( Figure 1) which improved water solubility as well as Human islet amyloid polypeptide aggregation activity. [23] We have synthesized pyrazole curcumin disodium acetate (PyCurOAc) and studied its AGE inhibitory activity, both in vitro and in vivo using C.elegans as an animal model. The possible mechanistic pathway for the AGE inhibition activity of PyCur-OAc has also been confirmed.…”

Section: Introductionmentioning

confidence: 99%

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Synthesis of a Water‐Soluble Pyrazole Curcumin Derivative: In Vitro and In Vivo AGE Inhibitory Activity and Its Mechanism

et al. 2017

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The new chemical entity, water‐soluble pyrazole curcumin derivative (PyCurOAc) was designed, synthesized and characterized for the purpose of inhibition of AGE formation. The compound showed an excellent in vitro AGEs inhibition activity than curcumin itself as well as the standard. Further, the AGE inhibition activity was substantiated in vivo using C.elegans as an animal model. The mechanistic investigation for the inhibition of AGEs with PyCurOAc was studied with glod‐4 expressions in C.elegans and glucose trapping method. This study suggests that the synthesized compound could be used to treat the formation of AGEs in hyperglycemic nematodes and higher animals.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Synthesis of a Water‐Soluble Pyrazole Curcumin Derivative: In Vitro and In Vivo AGE Inhibitory Activity and Its Mechanism

et al. 2017

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“…In this context, substances interacting with surfaces of either virions or cells may show a decrease in HIV infection even if those substance do not bind to SEVI amyloid fibrils. For instance, a curcumin derivative, curcumin diacetate (CurDAc), was implicated to bind to membrane surfaces which, thus, may prevent binding of amyloid fibrils …”

Section: Inhibition Of Sevi‐enhanced Hiv Viral Infectionmentioning

confidence: 99%

“…For instance, a curcumin derivative, curcumin diacetate (CurDAc), was implicated to bind to membrane surfaces which, thus, may prevent binding of amyloid fibrils. 50 Nanoparticles, which were generated from a polymer comprising moieties of amyloid-binding 6methylbenzothiazole aniline with high affinity for SEVI amyloid fibrils and similar in size and shape to HIV virions, disabled SEVI-mediated HIV transmission in cells. 51 These nanoparticles and polymers were far more efficient for inhibiting SEVI-enhanced HIV infection than monomeric and pentameric 6methylbenzothiazole aniline, proposing a critical role of steric hindrance in the design of effective SEVI neutralizing agents.…”

Section: Development Of Agents To Suppress Hiv Interaction With Sevi mentioning

confidence: 99%

Semen‐derived amyloidogenic peptides—Key players of HIV infection

Lee

Ramamoorthy

2018

Protein Science

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Misfolding and amyloid aggregation of intrinsically disordered proteins (IDPs) are implicated in a variety of diseases. Studies have shown that membrane plays important roles on the formation of intermediate structures of IDPs that can initiate (and/or speed-up) amyloid aggregation to form fibers. The process of amyloid aggregation also disrupts membrane to cause cell death in amyloid diseases like Alzheimer's disease and type-2 diabetes. On the other hand, recent studies reported the membrane fusion properties of amyloid fibers. Remarkably, amyloid-fibril formation by short peptide fragments of highly abundant prostatic acidic-phosphatase (PAP) in human semen and are capable of boosting the rate of HIV infection up to 400,000-fold during sexual contact. Unlike the least toxic fully matured fibers of most amyloid proteins, the semen-derived enhancer of virus infection (SEVI) amyloid-fibrils of PAP peptide fragments are highly potent in rendering the maximum rate of HIV infection. This unusual property of amyloid fibers has witnessed increasing number of studies on the biophysical aspects of fiber formation and fiber-membrane interactions. NMR studies have reported a highly disordered partial helical structure in a membrane environment for the intrinsically disordered PAP peptide that promotes the fusion of the viral membrane with that of host cells. The purpose of this review article is to unify and integrate biophysical and immunological research reported in the previous studies on SEVI. Specifically, amyloid aggregation, dramatic HIV infection enhancing properties, membrane fusion properties, high resolution NMR structure, and approaches to eliminate the enhancement of HIV infection of SEVI peptides are discussed.

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“…The proteins involved in PCD are misfolded compared to their native state, and contain beta sheet rich structures termed as amyloid fibrils [4,5]. In view of the importance of protein fibrillation in various diseases, many efforts have been made to find molecules which can inhibit the fibrillation process [6–11]. …”

Section: Introductionmentioning

confidence: 99%

Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations

et al. 2016

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We report here interesting synergistic effects of proline and sorbitol, two well-known chemical chaperones, in the inhibition of fibrillation of two proteins, insulin and lysozyme. A combination of many biophysical techniques has been used to understand the structural morphology and modes of interaction of the chaperones with the proteins during fibrillation. Both the chaperones establish stronger polar interactions in the elongation and saturation stages of fibrillation compared to that in the native stage. However, when presented as a mixture, we also see contribution of hydrophobic interactions. Thus, a co-operative adjustment of polar and hydrophobic interactions between the chaperones and the protein surface seems to drive the synergistic effects in the fibrillation process. In insulin, this synergy is quantitatively similar in all the stages of the fibrillation process. These observations would have significant implications for understanding protein folding concepts, in general, and for designing combination therapies against protein fibrillation, in particular.

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Influence of a curcumin derivative on hIAPP aggregation in the absence and presence of lipid membranes

Cited by 67 publications

References 40 publications

Synthesis of a Water‐Soluble Pyrazole Curcumin Derivative: In Vitro and In Vivo AGE Inhibitory Activity and Its Mechanism

Synthesis of a Water‐Soluble Pyrazole Curcumin Derivative: In Vitro and In Vivo AGE Inhibitory Activity and Its Mechanism

Semen‐derived amyloidogenic peptides—Key players of HIV infection

Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations

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