Purification and partial characterization of a new lectin from Parkia panurensis Benth. ex H.C. Hopkins seeds (Leguminosae family; Mimosoideae subfamily) and evaluation of its biological effects

Cavada, Benildo Sousa; Bari, Alfa Umaro; Pinto-Junior, Vanir Reis; Lossio, Claudia Figueiredo; Silva, Mayara Torquato Lima; Souza, Luiz Augusto Gomes de; Oliveira, M. R. de; Souza-Filho, Claudio Henrique Dahne; Correia, Sarah Elizabeth Gomes; Vital, Ana Paula Moreira Sousa; Lima, Lara Dias; Osterne, Vinicius Jose Da Silva; Nascimento, Kyria S.

doi:10.1016/j.ijbiomac.2019.10.102

Cited by 15 publications

(15 citation statements)

References 30 publications

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“…Lectin activity was detected by hemagglutination assays, following the protocol described in Cavada et al [17]. Aliquots of 50 µL for each sample were 2-fold diluted in a 96-well plate containing 50 µL saline (150 mM NaCl, 5 mM CaCl2, 5 mM MnCl2), after which 50 µL 3% erythrocytes (rabbit and human -A, B, and O cells), both native and treated with proteolytic enzymes, were added.…”

Section: Hemagglutinating Activity (Ha) Sugar-inhibition Assays and C...mentioning

confidence: 99%

“…To verify whether CsL is dependent on divalent cations, the lectin solution was dialyzed against 150 mM NaCl containing 100 mM EDTA for 24 h, followed by an additional dialysis step against 150 mM NaCl to remove excess EDTA. Hemagglutination assays were then carried out in the presence and absence of CaCl2 and MnCl2, both at 10 mM [17].…”

Section: Physicochemical Characterizationmentioning

confidence: 99%

“…The data were processed and analyzed using ProteinLynx (Waters), and the search parameter was the peptide fragmentation pattern. The CID spectra were interpreted manually using the Peptide Sequencing tool of MassLynx 4.1 (Waters) software [17].…”

Section: Amino Acid Sequence Analysismentioning

confidence: 99%

“…Incubation was performed in glass flasks with 1 g of cysts per liter of seawater. After 48 hours, aeration was interrupted, and only highly motile Artemia nauplii were collected for trials [17].…”

Section: Glycan Array Analysesmentioning

confidence: 99%

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Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

Oliveira

Osterne

Lossio

et al. 2021

International Journal of Biological Macromolecules

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Section: Hemagglutinating Activity (Ha) Sugar-inhibition Assays and C...mentioning

confidence: 99%

Section: Physicochemical Characterizationmentioning

confidence: 99%

Section: Amino Acid Sequence Analysismentioning

confidence: 99%

Section: Glycan Array Analysesmentioning

confidence: 99%

See 2 more Smart Citations

Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

Oliveira

Osterne

Lossio

et al. 2021

International Journal of Biological Macromolecules

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“…It has an extensive regional representation as the state of Tocantins' symbol tree and also peculiar characteristics resulting from its location on the border between the Cerrado and the Brazilian Caatinga (Lorenzi, 2020;Tocantins, 2012). Despite the fact that its extracts and isolated actives, primarily from pods, are well-known in the fields of nutrition and pharmacology (gastrointestinal infections in animals), little is known about their therapeutic potential (Araújo et al, 2019;Cavada et al, 2020;Santos et al, 2018). There are reports of the presence of phenolic compounds, flavonoids, flavones, phytosteroids, condensed tannins, and saponins in this species.…”

Section: Introductionmentioning

confidence: 99%

Chemical investigation, toxic potential and acetylcholinesterase inhibitory effect of Parkia platycephala leaf and seed extracts

Fernandes¹,

Rodrigues²,

Panontin³

et al. 2021

J. Med. Plants Res.

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The present work evaluated the inhibitor potential of acetylcholinesterase, the preliminary toxicity and determination of active components of different leaf and seed extracts of Parkia platycephala. All extracts were obtained through hot extraction in a closed system (Soxhlet). To obtain the leaf and seed hexanic, methanolic, and ethanolic extracts (LHE, LME, LEE, and SHE, SME, and SEE), sequential extraction was performed on the same plant sample using hexane, methanol, and hydroethanol solution (70%). Preliminary Phytochemical analysis and the characterization by gas chromatography coupled to the mass spectrometer (GC-MS) was performed. The content of phenols total flavonoids and the antioxidant potential was then quantified.The preliminary toxicity against Artemia salina was also evaluated and the potential for acetylcholinesterase inhibition was determined. The presence of tannins, flavonoids, saponins, phytosterols/triterpenoids and alkaloids were detected in phytochemical analysis. The leaf extracts showed antioxidant potential, LEM (IC 50 = 30.19 ± 0.75 μg/ml) and LEE (IC 50 = 40.62 ± 0.65 μg/ml). The analysis by GC-MS indicated a diversity of volatile compounds, evidencing urs-12-ene (triterpenoid) and 1,2,3-benzenetriol (phenol) in the leaf extracts, and linoelaidic acid (fatty acid), (Z)-9-octadecenamide, tricycle [20.8.0.0 (7.16)] triacontane,1(22),7(16)-diepoxy-, (Z)-7-hexadecenal (fatty aldehyde) in the seed extracts. The preliminary toxicity analysis demonstrated that the use of P. platyceplaha leave and seeds for medicinal purposes is relatively safe. All the extracts inhibited acetylcholinesterase, compared to the physostigmine control, with IC 50 values in the range of 9.85 to 15.68 mg/ml. Thus, these data support the use of P. platycephala as a potential therapy for Alzheimer's disease.

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A galactoside-specific Dalbergieae legume lectin from seeds of Vataireopsis araroba (Aguiar) Ducke

Osterne

Oliveira²,

Schutter³

et al. 2022

Glycoconj J

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The Dalbergieae lectin group encompasses several lectins with significant differences in their carbohydrate specificities and biological properties. The current work reports on the purification and characterization of a GalNAc/Gal-specific lectin from Vataireopsis araroba (Aguiar) Ducke, designated as VaL. The lectin was purified from the seeds in a single step using guar gum affinity chromatography. The lectin migrated as a single band of about 35 kDa on SDS-PAGE and, in native conditions, occurs as a homodimer. The purified lectin is stable at temperatures up to 60 °C and in a pH range from 7 to 8 and requires divalent cations for its activity. Sugar-inhibition assays demonstrate the lectin specificity towards N-acetyl-D-galactosamine, Dgalactose and related sugars. Furthermore, glycan array analyses show that VaL interacts preferentially with glycans containing terminal GalNAc/Galβ1-4GlcNAc. Biological activity assays were performed using three insect cell lines: CF1 midgut cells from the spruce budworm Choristoneura fumiferana, S2 embryo cells from the fruit fly Drosophila melanogaster, and GutAW midgut cells from the corn earworm Helicoverpa zea. In vitro assays indicated a biostatic effect for VaL on CF1 cells, but not on S2 and GutAW cells. The lectin presented a biostatic effect by reducing the cell growth and inducing cell agglutination, suggesting an interaction with glycans on the cell surface. VaL has been characterized as a galactoside-specific lectin of the Dalbergieae tribe, with sequence similarity to lectins from Vatairea and Arachis.

show abstract

Purification and partial characterization of a new lectin from Parkia panurensis Benth. ex H.C. Hopkins seeds (Leguminosae family; Mimosoideae subfamily) and evaluation of its biological effects

Cited by 15 publications

References 30 publications

Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

Chemical investigation, toxic potential and acetylcholinesterase inhibitory effect of Parkia platycephala leaf and seed extracts

A galactoside-specific Dalbergieae legume lectin from seeds of Vataireopsis araroba (Aguiar) Ducke

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