Anti-HIV activity of olive leaf extract (OLE) and modulation of host cell gene expression by HIV-1 infection and OLE treatment

Lee‐Huang, Sylvia; Zhang, Li; Huang, Peng; Chang, Young‐Tae; Huang, Paul L.

doi:10.1016/s0006-291x(03)01292-0

Cited by 193 publications

(134 citation statements)

References 35 publications

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“…Digestion with trypsin yielded the four expected A␤ fragments: [1][2][3][4][5], [6 -16], [17][18][19][20][21][22][23][24][25][26][27][28], and [29 -40] following cleavage after arginine (R) or lysine (K) residues (Table 2), as well as partially cleaved fragments ( Table 3). The soft ESI ionization also enabled the detection of noncovalent interactions between sequential and nonsequential fragments.…”

Section: Resultsmentioning

confidence: 99%

“…Noncovalent interactions of peptide fragments with OE, added before digestion, were detected for the [17][18][19][20][21][22][23][24][25][26][27][28] fragment of A␤ (Figure 2) and the partially cleaved peptide fragments [6 -28] and [6 -40]. In addition, noncovalent complexes of OE with the [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19] fragment, derived from the chymotryptic activity of the enzyme, was also detected.…”

Section: Resultsmentioning

confidence: 99%

“…When OE was added into already digested A␤ samples with trypsin ( Similarly, ESI-MS analysis of the A␤-OE Glu-C digest yielded signals corresponding to the expected A␤ fragments [4 -11], [12][13][14][15][16][17][18][19][20][21][22], and [23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39][40] following cleavage at the carboxy-terminus of glutamic acid (E) residues (Table 2), and the noncovalent complexes between OE and the [4 -11] and [12][13][14][15][16][17][18][19][20][21][22] A␤ Glu-C fragments ( Figure 3). Interactions between OE and the partially cleaved peptide fragments [4 -40] and (Table 4) When OE was added into already digested A␤ samples with Glu-C (Table 4), ESI signals corresponded to ...…”

Section: Resultsmentioning

confidence: 99%

“…Interactions between OE and the partially cleaved peptide fragments [4 -40] and (Table 4) When OE was added into already digested A␤ samples with Glu-C (Table 4), ESI signals corresponded to the noncovalent interactions of OE with the [4 -11] A␤ fragment, the partially cleaved peptide fragments [ [1][2][3][4][5][6][7][8][9][10][11] and (Table 4), and the [(4 -11)ϩ (12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)] added A␤ fragments. Processing of the aforementioned mapping data derived from the two different digestion protocols utilized in this study revealed the important regions and residues for the noncovalent interaction between A␤ and OE.…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, OE and its metabolites have been shown to be potent against contemporary diseases, such as HIV [20,21] and osteoporosis [22,23]. Interestingly, in vitro [24] and epidemiological [25] studies demonstrated the positive impact of polyphenols on the onset of age-related disorders, such as dementia [26,27].…”

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confidence: 99%

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Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry

Bazoti

Bergquist

Markides

et al. 2008

J. Am. Soc. Mass Spectrom.

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Abnormal accumulation and aggregation of amyloid-␤-peptide (A␤) eventually lead to the formation and cerebral deposition of amyloid plaques, the major pathological hallmark in Alzheimer's disease (AD). Oleuropein (OE), an Olea europaea L. derived polyphenol, exhibits a broad range of pharmacological properties, such as antioxidant, anti-inflammatory, and antiatherogenic, which could serve as combative mechanisms against several reported pathways involved in the pathophysiology of AD. The reported noncovalent interaction between A␤ and OE could imply a potential antiamyloidogenic role of the latter on the former via stabilization of its structure and prevention of the adaptation of a toxic ␤-sheet conformation. The established ␤-sheet conformation of the A␤ hydrophobic carboxy-terminal region and the dependence of its toxicity and aggregational propensity on its secondary structure make the determination of the binding site between A␤ and OE highly important for assessing the role of the interaction. In this study, two different proteolytic digestion protocols, in conjunction with high-sensitivity electrospray ionization mass spectrometric analysis of the resulting peptide fragments, were used to determine the noncovalent binding site of OE on A␤ and revealed the critical regions for the interaction. and its aggregational properties depend on both the peptide concentration and conformation, as well as on the solution conditions and pH [2,3]. It has been reported that reduction of the A␤ production, by controlling the cleavage of the larger transmembrane amyloid precursor protein (APP), or inhibition of its aggregation by using small molecules, which may interact noncovalently with A␤ and stabilize its structure, could serve as preventive or therapeutic approaches against AD [4]. In general, interruption of noncovalent interactions between protein and peptides, or even more between proteins/peptides and ligands can cause abnormalities, which often lead to diseases [5]. One interaction of this kind has been established between the Olea europaea derived bioactive compound, oleuropein (OE), and A␤ by means of electrospray ionization mass spectrometry (ESI-MS) [6]. This interaction could prove potent in inhibiting its aggregation.OE is a polyphenol extracted from the fruits and leaves of Olea europaea L. and possesses a wide range of pharmacological properties, such as antioxidant [7][8][9], anti-inflammatory [10, 11], antiatherogenic [12-14], antibacterial [15][16][17], and anticancer [18,19]. Moreover, OE and its metabolites have been shown to be potent against contemporary diseases, such as HIV [20,21] and osteoporosis [22,23]. Interestingly, in vitro [24] and epidemiological [25] studies demonstrated the positive impact of polyphenols on the onset of age-related disorders, such as dementia [26,27].It is regarded that the pathophysiology of AD is tangled and many theories have been proposed to illumine its mechanism. Free radical reactions and oxidative stress [28,29], as well as unregulated immune response [30,3...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry

Bazoti

Bergquist

Markides

et al. 2008

J. Am. Soc. Mass Spectrom.

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Simultaneous quantification of oleuropein and its metabolites in rat plasma by liquid chromatography electrospray ionization tandem mass spectrometry

Bazoti

Gikas

Tsarbopoulos

2009

Biomedical Chromatography

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Oleuropein (OE) is the cardinal bioactive compound derived from Olea europaea and possesses numerous beneficial properties for human health. However, despite the plethora of analytical methods that have studied the biological fate of olive oil-derived bioactive compounds, no validated methodology has been published to date for the simultaneous determination of OE, along with all its major metabolites. In this study, a liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI MS/MS) method has been developed and validated for the quantification of OE, simultaneously with its main metabolites hydroxytyrosol, 2-(3,4-dihydroxyphenyl)acetic acid, 4-(2-hydroxyethyl)-2-methoxy-phenol or homovanillyl alcohol, 2-(4-hydroxy-3-methoxyphenyl)acetic acid or homovanillic acid, and elenolic acid in rat plasma matrix. Samples were analyzed by LC-ESI MS/MS prior to and after enzymatic treatment. A solid-phase extraction step with high mean recovery for all compounds was performed as sample pretreatment. Calibration curves were linear for all bioactive compounds over the range studied, while the method exhibited good accuracy, intra- and inter-day precision. The limit of detection was in the picogram range (per milliliterof plasma) for HT and OE and in the nanogram range (per milliliter of plasma) for the other analytes, and the method was simple and rapid. The developed methodology was successfully applied for the simultaneous quantification of OE and its aforementioned metabolites in rat plasma samples, thus demonstrating its suitability for pharmacokinetics, as well as bioavailability and metabolism studies.

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Oxidative stability of oils containing olive leaf extracts obtained by pressure, supercritical and solvent‐extraction

Jiménez

Masson

Barriga

et al. 2010

Euro J Lipid Sci & Tech

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The effect of the addition of olive leaf (Olea europaea, cv. Arbequina) extracts, i.e. hydroalcoholic (ethanol-water 1:1; OHE), juice (OJ) and supercritical fluid-CO 2 (OSFE) on the oxidative stability of vegetable oils with different unsaturation, such as soybean oil (SBO), canola oil (CO) and high oleic sunflower oil (HOSO), were studied at two concentrations (250 and 630 mg/kg oil, expressed as caffeic acid equivalent (CAE)). The extracts were characterized by the total phenolic content (Folin-Ciocalteau method), phenol chromatographic profiles (LC-MS) and antioxidant activity (DPPH). OHE showed the highest phenol content (7.7 mg CAE/mL) while OJ and OSFE showed values of 5.4 and 2.2 mg CAE/mL, respectively. Oleuropein and its derivatives were the major phenolic compounds identified in OHE. The addition of 630 mg CAE/kg oil of OHE and OSFE to HOSO, SBO and CO showed an antioxidant effect, increasing significantly the induction time (IT) ( p<0.05). That effect was highest when the system was more monounsaturated. In contrast, OJ showed a pro-oxidant effect for all oils systems for both concentration studied. This behaviour could be attributed to the diphenol oxidase (PPO) activity.

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Anti-HIV activity of olive leaf extract (OLE) and modulation of host cell gene expression by HIV-1 infection and OLE treatment

Cited by 193 publications

References 35 publications

Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry

Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry

Simultaneous quantification of oleuropein and its metabolites in rat plasma by liquid chromatography electrospray ionization tandem mass spectrometry

Oxidative stability of oils containing olive leaf extracts obtained by pressure, supercritical and solvent‐extraction

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