Gallic acid is the major component of grape seed extract that inhibits amyloid fibril formation

Li, Yanqin; Pukala, Tara L.; Musgrave, Ian; Williams, Danielle M.; Dehle, Francis C.; Carver, John A.

doi:10.1016/j.bmcl.2013.09.071

Cited by 112 publications

(66 citation statements)

References 35 publications

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“…Interestingly, however, the addition of gallic acid to monomeric peptides inhibited fibril formation (Fig. 3, E and F), consistent with prior reports of gallic acid as a fibrillation inhibitor (21)(22)(23)(24)(25).…”

Section: Resultssupporting

confidence: 90%

“…1). Of these, three were previously uncharacterized, whereas the remaining one, gallic acid, is a natural component of grape seeds and has previously been reported to be an antagonist of several amyloid fibrils (23)(24)(25). We confirmed in a separate set of assays that gallic acid inhibits SP-mediated enhancement of HIV infection in the absence of inducing cellular toxicity (Fig.…”

Section: Resultssupporting

confidence: 68%

“…We identified from this screen the compound gallic acid, a phenol found in grape seed extract. Gallic acid has been shown to inhibit formation of ␣-synuclein, insulin, and amyloid-␤ amyloid fibrils (21)(22)(23)(24)(25). It is structurally related to the polyphenol epigallocatechin-3-gallate, a natural component found in green tea that was previously demonstrated to prevent formation of SEVI fibrils from PAPf39 monomers and to even degrade preformed fibrils (18,26,27).…”

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confidence: 99%

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Gallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection

LoRicco

Neidleman

et al. 2016

Journal of Biological Chemistry

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Recent in vitro studies have demonstrated that amyloid fibrils found in semen from healthy and HIV-infected men, as well as semen itself, can markedly enhance HIV infection rates. Semen fibrils are made up of multiple naturally occurring peptide fragments derived from semen. The best characterized of these fibrils are SEVI (semen-derived enhancer of viral infection), made up of residues 248 -286 of prostatic acidic phosphatase, and the SEM1 fibrils, made up of residues 86 -107 of semenogelin 1. A small molecule screen for antagonists of semen fibrils identified four compounds that lowered semen-mediated enhancement of HIV-1 infectivity. One of the four, gallic acid, was previously reported to antagonize other amyloids and to exert anti-inflammatory effects. To better understand the mechanism by which gallic acid modifies the properties of semen amyloids, we performed biophysical measurements (atomic force microscopy, electron microscopy, confocal microscopy, thioflavin T and Congo Red fluorescence assays, zeta potential measurements) and quantitative assays on the effects of gallic acid on semen-mediated enhancement of HIV infection and inflammation. Our results demonstrate that gallic acid binds to both SEVI and SEM1 fibrils and modifies their surface electrostatics to render them less cationic. In addition, gallic acid decreased semen-mediated enhancement of HIV infection but did not decrease the inflammatory response induced by semen. Together, these observations identify gallic acid as a non-polyanionic compound that inhibits semen-mediated enhancement of HIV infection and suggest the potential utility of incorporating gallic acid into a multicomponent microbicide targeting both the HIV virus and host components that promote viral infection.Amyloid fibrils are ordered protein aggregates associated with a large number of human diseases, many of which are neurodegenerative in nature, such as Alzheimer disease and Parkinson disease (1-3). They are characterized by their cross-␤ structure, with ␤ sheets running perpendicular to the fibril axis, and by their ability to bind to certain fluorescent dyes, such as thioflavin T (ThT), 4 whose fluorescence intensity increases considerably upon binding to amyloid fibrils.Amyloid fibrils are also found in semen from young, healthy men (4). Whether these fibrils serve a physiological function is not known, but they have been shown to markedly increase infection by a variety of sexually transmitted viruses, most notably HIV-1 (5-7). Under limiting dilution conditions, semen fibrils can increase HIV infection rates by up to 5 orders of magnitude (6). These fibrils are made up of naturally occurring peptide fragments in semen (6, 8 -10). The best characterized semen fibril is made up of a 39-residue fragment from human prostatic acid phosphatase (PAPf39) and has been termed SEVI (semen-derived enhancer of viral infection) (6). More recently, a second set of semen fibrils was identified from prostate-specific antigen-generated fragments of semenogelin (referred to collectivel...

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Section: Resultssupporting

confidence: 90%

Section: Resultssupporting

confidence: 68%

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confidence: 99%

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Gallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection

LoRicco

Neidleman

et al. 2016

Journal of Biological Chemistry

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“…GA is one of the most important antioxidant components of a healthy diet. The anti-inflammatory, antibiotic, antifungal and anticancer effects of GA are well known as well as its role in preventing cardiovascular diseases and neurodegenerative disorders [11][12][13][14][15]. Many GA-like compounds (phenolic acids) are present in large concentrations in different plants [16].…”

Section: Introductionmentioning

confidence: 99%

“…GA-like compounds are also used in biomedicine as drugs for toxic metal removal due to their capability of chelating heavy metal and transition metal ions [18]. Their application for curing degenerative diseases is promising, because they can cross the blood brain barrier and chelate toxic ions in the brain thus preventing or even inverting the formation of plaques [13,14]. When attached to magnetic nanoparticles, the curing efficiency can be enhanced via magnetic targeting.…”

Section: Introductionmentioning

confidence: 99%

Hemocompatibility and Biomedical Potential of Poly(Gallic Acid) Coated Iron Oxide Nanoparticles for Theranostic Use

Szekeres

Illés

Janko³

et al. 2015

J Nanomed Nanotechnol

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Myricetin Inhibits α‐Synuclein Amyloid Aggregation by Delaying the Liquid‐to‐Solid Phase Transition

Chen

et al. 2022

ChemBioChem

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The aggregation of α-synuclein (α-Syn) is a critical pathological hallmark of Parkinson's disease (PD). Prevention of α-Syn aggregation has become a key strategy for treating PD. Recent studies have suggested that α-Syn undergoes liquid-liquid phase separation (LLPS) to facilitate nucleation and amyloid formation. Here, we examined the modulation of α-Syn aggregation by myricetin, a polyhydroxyflavonol compound, under the conditions of LLPS. Unexpectedly, neither the initial morphology nor the phase-separated fraction of α-Syn was altered by myricetin. However, the dynamics of α-Syn con-densates decreased upon myricetin binding. Further studies showed that myricetin dose-dependently inhibits amyloid aggregation in the condensates by delaying the liquid-to-solid phase transition. In addition, myricetin could disassemble the preformed α-Syn amyloid aggregates matured from the condensates. Together, our study shows that myricetin inhibits α-Syn amyloid aggregation in the condensates by retarding the liquid-to-solid phase transition and reveals that α-Syn phase transition can be targeted to inhibit amyloid aggregation. www.chembiochem.org

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Gallic acid is the major component of grape seed extract that inhibits amyloid fibril formation

Cited by 112 publications

References 35 publications

Gallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection

Gallic Acid Is an Antagonist of Semen Amyloid Fibrils That Enhance HIV-1 Infection

Hemocompatibility and Biomedical Potential of Poly(Gallic Acid) Coated Iron Oxide Nanoparticles for Theranostic Use

Myricetin Inhibits α‐Synuclein Amyloid Aggregation by Delaying the Liquid‐to‐Solid Phase Transition

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