Artocarpus Integer Research Articles

Assessment of Antioxidant Capacity and Cytotoxicity of Selected Malaysian Plants

Thirteen Malaysian plants; Artocarpus champeden, Azadirachta indica, Fragaria x ananassa, Garcinia mangostana, Lawsonia inermis, Mangifera indica, Nephelium lappaceum, Nephelium mutobile, Peltophorum pterocarpum, Psidium guajava and Syzygium aqueum, selected for their use in traditional medicine, were subjected to a variety of assays. Antioxidant capability, total phenolic content, elemental composition, as well as it cytotoxity to several cell lines of the aqueous and ethanolic extracts from different parts of these selected Malaysian plants were determined. In general, the ethanolic extracts were better free radical scavengers than the aqueous extracts and some of the tested extracts were even more potent than a commercial grape seed preparation. Similar results were seen in the lipid peroxidation inhibition studies. Our findings also showed a strong correlation of antioxidant activity with the total phenolic content. These extracts when tested for its heavy metals content, were found to be below permissible value for nutraceutical application. In addition, most of the extracts were found not cytotoxic to 3T3 and 4T1 cells at concentrations as high as 100 μg/mL. We conclude that although traditionally these plants are used in the aqueous form, its commercial preparation could be achieved using ethanol since a high total phenolic content and antioxidant activity is associated with this method of preparation.

Crystallization and preliminary structural studies of champedak galactose-binding lectin.

Galactose-binding lectin from champedak (Artocarpus integer) consists of two chains: alpha and beta (133 and 21 amino acids, respectively). It has been shown to recognize and bind to carbohydrates involved in IgA and C1 inhibitor molecules. The protein was purified and crystallized at 293 K. Crystals were observed in two space groups, P2(1) and P2(1)2(1)2, and diffracted to 1.65 and 2.6 A, respectively.

In vitro starch hydrolysis and estimated glycaemic index of bread substituted with different percentage of chempedak (Artocarpus integer) seed flour

Chempedak (Artocarpus integer) seed flour (CSF) was substituted for wheat flour at different levels (0%, 10%, 20%, 30% w/w) in bread. Assessment on the in vitro starch hydrolysis was carried out to evaluate the hydrolysis index (HI) and estimated glycaemic index (EGI) of bread substituted with different levels of CSF. Kinetics of in vitro starch hydrolysis in all bread samples (with the exception for white bread) indicated a gradual increase with respect to time intervals. Bread of 30% CSF exhibited significantly lower (p < 0.05) in vitro starch hydrolysis, as compared with the other samples. Results showed that HI value decreased significantly (p < 0.05) as the levels of CSF substitution increased. Resistant starch (RS) content in bread samples was inversely related with HI value as CSF substitution levels increased, thus lowering the EGI value.

Artopeden A, a New Antiplasmodial Isoprenylated Flavone from Artocarpus champeden

A new isoprenylated flavone, artopeden A (1) was isolated from the barks of Artocarpus champeden (Moraceae), and the structure was elucidated by NMR spectral analysis. Artopeden A (1) showed a potent antiplasmodial activity with an IC 50 of 0.045 μg/mL against Plasmodium falciparum 3D7.

Drying Kinetics, Texture, Color, and Determination of Effective Diffusivities During Sun Drying of Chempedak

Sun drying of chempedak (Artocarpus integer) was carried out on different sample sizes to investigate the effects on product quality. Fick's second law model was used to determine the effective diffusivities of sun–dried chempedak slabs based on the drying rate versus moisture content plots. In addition, texture degradation and total color changes were investigated. The texture and color changes of dried chempedak were relatively significant (p < 0.05) compared to fresh chempedak. There was an increase in dried fruit hardness and chewiness but a decrease in springiness and cohesiveness during drying.

Drying kinetics and product quality of dried Chempedak

The objective of this study was to investigate the drying kinetics of chempedak (Artocarpus integer) at different drying temperatures (50°C, 60°C, 70°C) and slab dimensions. The drying data were fitted to the different semi-theoretical models based on moisture ratio (MR) to predict the drying kinetics. A logarithmic model was found to be the best fit in this study for all the drying temperatures tested. Effective diffusivities were estimated from Fick’s 2nd law and the Arrhenius equation was used to determine the diffusivity constant (Do) and activation energy (Ea). The texture and color of dried product were altered significantly during drying. The total color change (ΔE), hardness and chewiness were found to be increased with elevated temperature; meanwhile, springiness and cohesiveness of dried chempedak were relatively constant.

Some Properties of Starch Extracted from Three Thai Aromatic Fruit Seeds

AbstractStarches extracted from three Thai aromatic fruit seed, chempedak (Artocarpus integer), jackfruit (Artocarpus heterophyllus L.), and durian (Durio zibethinus L./ Murr) – with mung bean starch for comparison – were investigated for chemical compositions, amylose content, resistant starch content, granule morphology and size distribution, crystalline pattern, swelling power and solubility, pasting and thermal properties. The extracted starches were of very high purity. The fruit seed starches had lower amylose contents and much smaller granule size than mung bean starch and hence lower pasting viscosities. Chempedak and jackfruit seed starches were very similar in swelling power, solubility, gelatinization temperature and enthalpy, while the properties of durian seed starch were close to those of mung bean starch. The information obtained in this work could be very useful for food, pharmaceutical and cosmetics applications. Further study on other functional and molecular properties should be considered.

Prenylated 2-Arylbenzofurans from Two Species of Artocarpus

Two prenylated 2-arylbenzofurans, artoindonesianins A-1 and B-1, have been isolated from Artocarpus champeden and A. altilis, respectively, along with the known flavones cyclocommunol and cycloartocarpin, and a known stilbene, artoindonesianin F. The structures of these compounds were determined based on spectroscopic evidence. The chemotaxonomic significance of the presence of 2-arylbenzofuran derivatives in Artocarpus is briefly discussed.

Galactose-binding lectin from the seeds of champedak ( Artocarpus integer): sequences of its subunits and interactions with human serum O-glycosylated glycoproteins

Our group has previously reported the isolation, partial characterisation, and application of a Galβ1–3GalNAc- and IgA1-reactive lectin from the seeds of champedak ( Artocarpus integer). In the present study, we have subjected the purified lectin to reverse-phase high performance liquid chromatography and sequenced its subunits. Determination of the N-terminal sequence of the first 47 residues of the large subunit demonstrated at least 95% homology to the N-terminal sequence of the α chains of a few other galactose-binding Artocarpus lectins. The two smaller subunits of the lectin, each comprised of 21 amino acid residues, demonstrated minor sequence variability. Their sequences were generally comparable to the β chains of the other galactose-binding Artocarpus lectins. When used to probe human serum glycopeptides that were separated by two-dimensional gel electrophoresis, the lectin demonstrated strong apparent interactions with glycopeptides of IgA1, hemopexin, α 2-HS glycoprotein, α 1-antichymotrypsin, and a few unknown glycoproteins. Immobilisation of the lectin to Sepharose generated an affinity column that may be used to isolate the O-glycosylated serum glycoproteins.

THE APPLICATION OF ARTOCARPUS INTEGER SEED LECTIN-M IN THE DETECTION AND ISOLATION OF SELECTIVE HUMAN SERUM ACUTE-PHASE PROTEINS AND IMMUNOGLOBULINS

Champedak (Artocarpus integer) lectin-M is a lectin with high specificity and affinity for the core-mannosyl residues of the N-linked oligosaccharides of glycoproteins. We have studied the interaction of the champedak seed lectin with human serum glycoproteins that were resolved by 2-dimensional (2-D) gel electrophoresis. The lectin demonstrated strong interaction with haptoglobin β chain, orosomucoid, α1-antitrypsin, α2-HS glycoprotein, transferrin, hemopexin, α1B-glycoprotein, and the heavy chains of IgA, IgM and IgG of the human serum. With exceptions of the heavy chains of the immunoglobulins and α1B-glycoprotein, all the other lectin-M-probed glycopeptides are acute-phase proteins. The use of champedak lectin-M to probe for serum glycoproteins that were separated in a 2-D gel electrophoresis and Western blotting technique may be conveniently applied to analyse the acute-phase and humoral immune responses simultaneously. Subjecting human serum to immobilised-lectin-M affinity chromatography was able to isolate intact haptoglobin, α1-antitrypsin, α1B-glycoprotein, hemopexin and IgA.

An antimalarial stilbene from Artocarpus integer

Antimalarial activity-guided study of the aerial parts of Artocarpus integer led to the isolation of the prenylated stilbene, trans-4-(3-methyl- E-but-1-enyl)-3,5,2′,4′- tetrahydroxystilbene with an EC 50 of 1.7 μg/ml against Plasmodium falciparum in culture. The known stilbenes, trans-4-isopentenyl-3,5,2′,4′-tetrahydroxystilbene and 4-methoxy-2,2-dimethyl-6-(2-(2,4-dihydroxy)phenyl- trans-ethenyl)chromene, were also isolated. Structures of these compounds were deduced on the basis of their spectral data.

Artocarpus (Moraceae)–gall midge pollination mutualism mediated by a male‐flower parasitic fungus

A previously undescribed pollination system involving a monoecious tree species, Artocarpus integer (Moraceae), pollinator gall midges, and fungi is reported from a mixed dipterocarp forest in Sarawak, Borneo. The fungus Choanephora sp. (Choanephoraceae, Mucorales, Zygomycetes) infects male inflorescences of A. integer, and gall midges (Contarinia spp., Cecidomyiinae, Diptera) feed on the fungal mycelia and oviposit on the inflorescence. Their larvae also feed on the mycelia and pupate in the inflorescence. The gall midges are also attracted by female inflorescences lacking mycelia, probably due to a floral fragrance similar to that of male inflorescences. Because of the sticky pollen, dominance of Contarinia spp. in flower visitors, and pollen load observed on Contarinia spp. collected on both male and female inflorescences, Artocarpus integer is thought to be pollinated by the gall midges. Although several pathogenic fungi have been reported to have interactions with pollinators, this is the first report on a pollination mutualism in which a fungus plays an indispensable role. The pollination system described here suggests that we should be more aware of the roles fungi can play in pollinations.

Artoindonesianins A and B, two new prenylated flavones from the root of Artocarpus champeden.

Two new prenylated flavones, named artoindonesianin A (1) and artoindonesianin B (2), were isolated from the root of Artocarpus champeden, together with a known prenylated flavone, artonin A. The structures of artoindonesianins A and B were determined on the basis of spectral evidence (MS, 1H and 13C NMR) and by comparison with known related compounds. Compounds 1 and 2 exhibited cytotoxic activity against murine leukemia (P-388) cells.

Effect of the mannose-binding artocarpus integer lectin on the cellular proliferation of murine lymphocytes

The effect of the mannose-binding champedak (Artocarpus integer) lectin-M on the cellular proliferation of murine lymphocytes was investigated in this study. Our data demonstrated that the lectin was the main mitogenic component in the crude extract of the champedak seeds. It stimulated the proliferation of murine T cells at an optimal concentration of 2.5 μg/ml in a 3 day culture. Lectin-M appeared to be a T-cell mitogen as it does not induce significant DNA synthesis when cultured with spleen cells from the nude mouse. In the absence of T cells, the lectin was incapable of inducing resting B cells to differentiate into immunoglobulin secreting plasma cells.

Isolation of a mannose-binding and IgE- and IgM-reactive lectin from the seeds of Artocarpus integer

A mannose-binding lectin, termed champedak lectin-M, was isolated from an extract of the crude seeds of champedak ( Artocarpus integer). On gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kDa. SDS-PAGE showed the mannose-binding lectin to be composed of 16.8 kDa polypeptides with some of the polypeptides being disulphide-linked to give dimers. When tested with all isotypes of immunoglobulins, champedak lectin-M demonstrated a selective strong interaction with human IgE and IgM, and a weak interaction with IgA2. The binding interactions of lectin-M were metal ion independent. The lectin was also shown to interact with horseradish peroxidase, ovalbumin, porcine thyroglobulin, human α 1-acid glycoprotein, transferrin and α 1-antitrypsin. It demonstrated a binding preference to Man α1–3Man ligands in comparison to Man α1–6Man or Man α1–2Man.

Reactions in reactive sintering of aluminium-titanium diboride composites: J. Duszczyk et al.(Delft University of Technology, The Netherlands)

A mannose-binding lectin, termed champedak lectin-M, was isolated from an extract of the crude seeds of champedak (Artocarpus integer). On gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kDa. SDS-PAGE showed the mannose-binding lectin to be composed of 16.8 kDa polypeptides with some of the polypeptides being disulphide-linked to give dimers. When tested with all isotypes of immunoglobulins, champedak lectin-M demonstrated a selective strong interaction with human IgE and IgM, and a weak interaction with IgA2. The binding interactions of lectin-M were metal ion independent. The lectin was also shown to interact with horseradish peroxidase, ovalbumin, porcine thyroglobulin, human α1-acid glycoprotein, transferrin and α1-antitrypsin. It demonstrated a binding preference to Manα1–3Man ligands in comparison to Manα1–6Man or Manα1–2Man.

A New Prenylated Flavone from Artocarpus champeden

Abstract: A new prenylated flavone, named cyclochampedol (1), together with four known triterpenesscycloeucalenol, glutinol, cycloartenone, and 24-methylenecycloartanonesas well as β-sitosterol were isolated from Artocarpus champeden. The structure of the new compound was determined on the basis of spectral evidence and by comparison with known related compounds. Compound 1 is active in the brine shrimp lethality assay.

Effect of Artocarpus integer lectin on functional activity of guinea-pig complement.

The effect of Artocarpus integer lectin (lectin C) on the functional activity of guinea-pig complement was investigated. Purified and crude extract of lectin C from six cultivars of Artocarpus integer seeds were found to consume complement and thus decreased the complement-induced haemolytic activity of sensitized sheep erythrocytes. The change in the complement-mediated haemolytic activity was significantly decreased when incubation of the lectins was performed in the presence of melibiose. The reversal effect of the carbohydrate, which is a potent inhibitor of the lectin's binding to O-linked oligosaccharides of glycoprotein, demonstrate involvement of the lectins interaction with O-glycans of glycoproteins in the consumption of guinea-pig complement.

The α- and β-subunits of the jacalins are cleavage products from a 17-kDa precursor

The jacalins of three Artocarpus species were purified by affinity chromatography on a desialylated mucin-CNBr-Sepharose 4B column. The β-chains and the 14 kDa α-chains were separated by high pressure liquid chromatography and the 17 kDa and the 17 kDa chains by preparative electrophoresis. The 17 kDa and 14 kDa chains had a similar highly conserved N-terminal sequence. The β-chains were different for the three species and Artocarpus champeden contained two different β-chains. CNBr cleavage of the 17 kDa polypeptide of Artocarpus tonkinensis yielded one peptide more than the 14 kDa. The N-terminal sequence of this fragment was similar to that of the β-chain proving that this chain results from a proteolytic cleavage at the C-terminus of the 17 kDa peptide. The large heterogeneity of the β-chains of jacalins from different species could be used as a marker for evolutionary studies on the Artocarpus family.

Iga binding lectins isolated from distinct artocarpus species demonstrate differential specificity

The discovery of jacalin, a group of lectins from jackfruit seeds ( Artocarpus heterophyllus), has attracted considerable attention due to its numerous interesting immunological properties as well as its usefulness in the isolation of various serum proteins. We have further identified a similar lectin from the seeds of Champedak ( Artocarpus integer) which we refer to as lectin-C and performed comparative studies with two types of jacalin isolated from different batches of the Malaysian jackfruit seeds (jacalin-Ml and jacalin-M2). The three purified lectins demonstrated equivalent apparent M r of about 52,500, each of which comprised of a combination of two types of non-covalently-linked subunits with apparent M r of approximately 13,300 and 16,000. The lectins demonstrated equal haemagglutinating activity against human erythrocytes of blood groups A, B, AB and O. Our data also demonstrated that lectin-C, jacalin-Ml and jacalin-M2 are similar by selectively precipitating human serum IgA1 and colostral slgA but not IgA2, IgD, IgG and IgM. When immunoelectrophoresis was performed on normal human sera and reacted with the lectins, single precipitin arcs corresponding to IgA immunoprecipitates were detected with lectin-C and jacalin-MI. Jacalin-M2, however, exhibited two closely associated precipitin arcs. The binding of these lectins with IgA was pronouncely inhibited in the presence of p-nitrophenyl-β- d-galactopyranoside, 1- o-methyl-α- d-galactopyranoside, d-melibiose, N-acetyl- d-galactosamine and d-galactose. The data therefore provide evidence on the differential specificity of IgA binding lectins isolated from seeds of similar as well as distinct Artocarpus species.