Displaying publications 81 - 100 of 382 in total

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  1. Fulltext Can Renin-Angiotensin System Inhibitors Protect Against Acute Kidney Injury in Patients With COVID-19?
    Kow CS, Ramachandram DS, Hasan SS
    Crit Care Med, 2022 Nov 01;50(11):e796-e797.
    PMID: 36227048 DOI: 10.1097/CCM.0000000000005618
    Matched MeSH terms: Angiotensin-Converting Enzyme Inhibitors/pharmacology; Angiotensin-Converting Enzyme Inhibitors/therapeutic use
  2. Fulltext Aromatic compounds and organic acids identified from Ganoderma formosanum exhibit synergistic anti-melanogenic effects
    Hsieh CC, Hou CY, Lei HY, Khumsupan D, Chai HJ, Lim PK, et al.
    J Food Drug Anal, 2024 Dec 15;32(4):532-543.
    PMID: 39752867 DOI: 10.38212/2224-6614.3509
    This study reveals the anti-tyrosinase activity of Ganoderma formosanum extracts, pinpointing compounds including gluconic acid, mesalamine, L-pyroglutamic acid, esculetin, 5-hydroxyindole, and salicylic acid, as effective melanin production inhibitors in melanoma cells and zebrafish embryos. Furthermore, multiple molecular docking simulations provided insights into interactions between the identified compounds and tyrosinase, increasing binding affinity up to -16.36 kcal/mol. The enhanced binding of identified compounds to tyrosinase facilitated synergistic inhibitory effects on melanin production. This study highlights the potential of GFE-EA as a source of natural tyrosinase inhibitors and contributes to understanding the role of active compounds extracted from G. formosanum.
    Matched MeSH terms: Enzyme Inhibitors/pharmacology; Enzyme Inhibitors/chemistry
  3. Design, synthesis, in vitro evaluation, molecular docking and ADME properties studies of hybrid bis-coumarin with thiadiazole as a new inhibitor of Urease
    Alomari M, Taha M, Imran S, Jamil W, Selvaraj M, Uddin N, et al.
    Bioorg Chem, 2019 11;92:103235.
    PMID: 31494327 DOI: 10.1016/j.bioorg.2019.103235
    Hybrid bis-coumarin derivatives 1-18 were synthesized and evaluated for their in vitro urease inhibitory potential. All compounds showed outstanding urease inhibitory potential with IC50 value (The half maximal inhibitory concentration) ranging in between 0.12 SD 0.01 and 38.04 SD 0.63 µM (SD standard deviation). When compared with the standard thiourea (IC50 = 21.40 ± 0.21 µM). Among these derivatives, compounds 7 (IC50 = 0.29 ± 0.01), 9 (IC50 = 2.4 ± 0.05), 10 (IC50 = 2.25 ± 0.05) and 16 (IC50 = 0.12 ± 0.01) are better inhibitors of the urease compared with thiourea (IC50 = 21.40 ± 0.21 µM). To find structure-activity relationship molecular docking as well as absorption, distribution, metabolism, and excretion (ADME) studies were also performed. Various spectroscopic techniques like 1H NMR, 13C NMR, and EI-MS were used for characterization of all synthesized analogs. All compounds were tested for cytotoxicity and found non-toxic.
    Matched MeSH terms: Enzyme Inhibitors/chemical synthesis*; Enzyme Inhibitors/metabolism; Enzyme Inhibitors/pharmacology; Enzyme Inhibitors/chemistry
  4. Bi-heterocyclic benzamides as alkaline phosphatase inhibitors: Mechanistic comprehensions through kinetics and computational approaches
    Abbasi MA, Nazir M, Ur-Rehman A, Siddiqui SZ, Hassan M, Raza H, et al.
    Arch Pharm (Weinheim), 2019 Mar;352(3):e1800278.
    PMID: 30624805 DOI: 10.1002/ardp.201800278
    Novel bi-heterocyclic benzamides were synthesized by sequentially converting 4-(1H-indol-3-yl)butanoic acid (1) into ethyl 4-(1H-indol-3-yl)butanoate (2), 4-(1H-indol-3-yl)butanohydrazide (3), and a nucleophilic 5-[3-(1H-indol-3-yl)propyl]-1,3,4-oxadiazole-2-thiol (4). In a parallel series of reactions, various electrophiles were synthesized by reacting substituted anilines (5a-k) with 4-(chloromethyl)benzoylchloride (6) to afford 4-(chloromethyl)-N-(substituted-phenyl)benzamides (7a-k). Finally, the nucleophilic substitution reaction of 4 was carried out with newly synthesized electrophiles, 7a-k, to acquire the targeted bi-heterocyclic benzamides, 8a-k. The structural confirmation of all the synthesized compounds was done by IR, 1 H NMR, 13 C NMR, EI-MS, and CHN analysis data. The inhibitory effects of these bi-heterocyclic benzamides (8a-k) were evaluated against alkaline phosphatase, and all these molecules were identified as potent inhibitors relative to the standard used. The kinetics mechanism was ascribed by evaluating the Lineweaver-Burk plots, which revealed that compound 8b inhibited alkaline phosphatase non-competitively to form an enzyme-inhibitor complex. The inhibition constant Ki calculated from Dixon plots for this compound was 1.15 μM. The computational study was in full agreement with the experimental records and these ligands exhibited good binding energy values. These molecules also exhibited mild cytotoxicity toward red blood cell membranes when analyzed through hemolysis. So, these molecules might be deliberated as nontoxic medicinal scaffolds to render normal calcification of bones and teeth.
    Matched MeSH terms: Enzyme Inhibitors/chemical synthesis*; Enzyme Inhibitors/pharmacology; Enzyme Inhibitors/toxicity; Enzyme Inhibitors/chemistry
  5. Fulltext Angiotensin-I Converting Enzyme (ACE) Inhibitory and Anti-Oxidant Activities of Sea Cucumber (Actinopyga lecanora) Hydrolysates
    Ghanbari R, Zarei M, Ebrahimpour A, Abdul-Hamid A, Ismail A, Saari N
    Int J Mol Sci, 2015 Dec 04;16(12):28870-85.
    PMID: 26690117 DOI: 10.3390/ijms161226140
    In recent years, food protein-derived hydrolysates have received considerable attention because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive and anti-oxidative activities are receiving special attention as both activities can play significant roles in preventing cardiovascular diseases. The present study investigated the angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities of Actinopyga lecanora (A. lecanora) hydrolysates, which had been prepared by alcalase, papain, bromelain, flavourzyme, pepsin, and trypsin under their optimum conditions. The alcalase hydrolysate showed the highest ACE inhibitory activity (69.8%) after 8 h of hydrolysis while the highest anti-oxidative activities measured by 2,2-diphenyl 1-1-picrylhydrazyl radical scavenging (DPPH) (56.00%) and ferrous ion-chelating (FIC) (59.00%) methods were exhibited after 24 h and 8 h of hydrolysis, respectively. The ACE-inhibitory and anti-oxidative activities displayed dose-dependent trends, and increased with increasing protein hydrolysate concentrations. Moreover, strong positive correlations between angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities were also observed. This study indicates that A. lecanora hydrolysate can be exploited as a source of functional food owing to its anti-oxidant as well as anti-hypertension functions.
    Matched MeSH terms: Angiotensin-Converting Enzyme Inhibitors/pharmacology*; Angiotensin-Converting Enzyme Inhibitors/chemistry*
  6. Inhibition by toxic compounds in the hemicellulosic hydrolysates on the activity of xylose reductase from Candida tropicalis
    Rafiqul IS, Sakinah AM, Zularisam AW
    Biotechnol Lett, 2015 Jan;37(1):191-6.
    PMID: 25214231 DOI: 10.1007/s10529-014-1672-5
    Xylose reductase (XR) is an oxidoreductase having potential applications in the production of various specialty products, mainly xylitol. It is important to screen for compounds that can decrease XR activity and consequently can decrease xylitol production. We have identified the byproducts in the hemicellulosic hydrolysate that inhibit XR from Candida tropicalis and measured their effects. XR inhibitory activities of byproducts, glucose, acetic acid, arabinose, lignin-degradation products (LDPs), furfural and hydroxymethylfurfural (HMF), were evaluated by measuring the MIC and IC50 values. XR activity was 11.2 U/ml. Acetic acid, LDPs, furfural and HMF significantly inhibited XR with IC50 values of 11, 6.4, 2.3 and 0.4 g/l, respectively. This is the first report on the inhibitory activities of several byproducts for XR.
    Matched MeSH terms: Enzyme Inhibitors/analysis; Enzyme Inhibitors/metabolism
  7. Chemical profile and antiacetylcholinesterase, antityrosinase, antioxidant and α-glucosidase inhibitory activity of Cynometra cauliflora L. leaves
    Ado MA, Abas F, Ismail IS, Ghazali HM, Shaari K
    J Sci Food Agric, 2015 Feb;95(3):635-42.
    PMID: 25048579 DOI: 10.1002/jsfa.6832
    The aim of the current study was (i) to evaluate the bioactive potential of the leaf methanolic extract of Cynometra cauliflora L., along with its respective hexane, dichloromethane, ethyl acetate (EtOAc), n-butanol (n-BuOH) and aqueous fractions, in inhibiting the enzymes α-glucosidase, acetylcholinesterase (AChE) and tyrosinase as well as evaluating their antioxidant activities. (ii) In addition, in view of the limited published information regarding the metabolite profile of C. cauliflora, we further characterized the profiles of the EtOAc and n-BuOH fractions using liquid chromatography-diode array detection-electrospray ionization-tandem mass spectrometry.
    Matched MeSH terms: Enzyme Inhibitors/analysis; Enzyme Inhibitors/pharmacology*
  8. GC-MS-based metabolite profiling of Cosmos caudatus leaves possessing alpha-glucosidase inhibitory activity
    Javadi N, Abas F, Abd Hamid A, Simoh S, Shaari K, Ismail IS, et al.
    J Food Sci, 2014 Jun;79(6):C1130-6.
    PMID: 24888400 DOI: 10.1111/1750-3841.12491
    Cosmos caudatus, which is known as "Ulam Raja," is an herbal plant used in Malaysia to enhance vitality. This study focused on the evaluation of the α-glucosidase inhibitory activity of different ethanolic extracts of C. caudatus. Six series of samples extracted with water, 20%, 40%, 60%, 80%, and 100% ethanol (EtOH) were employed. Gas chromatography-mass spectrometry (GC-MS) and orthogonal partial least-squares (OPLS) analysis was used to correlate bioactivity of different extracts to different metabolite profiles of C. caudatus. The obtained OPLS scores indicated a distinct and remarkable separation into 6 clusters, which were indicative of the 6 different ethanol concentrations. GC-MS can be integrated with multivariate data analysis to identify compounds that inhibit α-glucosidase activity. In addition, catechin, α-linolenic acid, α-D-glucopyranoside, and vitamin E compounds were identified and indicate the potential α-glucosidase inhibitory activity of this herb.
    Matched MeSH terms: Enzyme Inhibitors/analysis; Enzyme Inhibitors/pharmacology*
  9. Mechanisms of angiotensin converting enzyme inhibitor-induced IOP reduction in normotensive rats
    Agarwal R, Krasilnikova AV, Raja IS, Agarwal P, Mohd Ismail N
    Eur J Pharmacol, 2014 May 5;730:8-13.
    PMID: 24583339 DOI: 10.1016/j.ejphar.2014.02.021
    Angiotensin converting enzyme inhibitors (ACEIs) have been shown to lower intraocular pressure (IOP). Since, the ACEIs cause increased tissue prostaglandin levels, we hypothesized that the mechanisms of ACEI-induced IOP reduction have similarity with those of prostaglandin analogs. The present study investigated the involvement of matrix metalloproteinases (MMPs) and cytokine activity modulation as the underlying mechanisms of ACEI-induced ocular hypotension. The IOP lowering effect of single drop of enalaprilat dehydrate 1% was evaluated in rats pretreated with a broad spectrum MMP inhibitor or a cytokine inhibitor. Effect of angiotensin receptor blocker, losartan potassium 2%, was also studied to evaluate involvement of angiotensin II receptor type 1 (AT1) in IOP lowering effect of ACEI. Topical treatment with single drop of enalaprilat resulted in significant IOP reduction in treated eye with mean peak reduction 20.3% at 3h post-instillation. Treatment with losartan resulted in a peak IOP reduction of 13.3%, which was significantly lower than enalaprilat, indicating involvement of mechanisms in addition to AT1 blockade. Pretreatment with a broad spectrum MMP inhibitor or a cytokine inhibitor significantly attenuated the enalprilat-induced IOP reduction with mean peak IOP reduction of 11.2% and 13.6% respectively. The IOP-lowering effect of enalaprilat seems to be attributed to reduced angiotensin II type 1 receptor stimulation and modulation of MMP and cytokines activities.
    Matched MeSH terms: Angiotensin-Converting Enzyme Inhibitors/administration & dosage; Angiotensin-Converting Enzyme Inhibitors/pharmacology*
  10. Winged bean [Psophorcarpus tetragonolobus (L.) DC] seeds as an underutilised plant source of bifunctional proteolysate and biopeptides
    Yea CS, Ebrahimpour A, Hamid AA, Bakar J, Muhammad K, Saari N
    Food Funct, 2014 May;5(5):1007-16.
    PMID: 24658538 DOI: 10.1039/c3fo60667h
    Hypertension is one of the major causes of cardiovascular-related diseases, which is highly associated with angiotensin-I-converting enzyme (ACE) activity and oxidative stress. In this study, winged bean seed (WBS), a potential source of protein, was utilised for the production of bifunctional proteolysate and biopeptides with ACE inhibitory and antioxidative properties. An enzymatic approach was applied, coupled with pretreatment of shaking and centrifuging techniques to remove endogenous ACE inhibitors prior to proteolysis. ACE inhibition reached its highest activity, 78.5%, after 12 h proteolysis while antioxidative activities, determined using assays involving DPPH˙ radical scavenging activity and metal ion-chelating activity, reached peaks of 65.0% and 65.7% at 8 h and 14 h, respectively. The said bioactivities were proposed to share some common structural requirements among peptides. A two-dimensional approach was employed for characterisation of effective peptides based on hydrophobicity, using RP-HPLC, and isoelectric property, using isoelectric focusing technique. Results revealed that acidic and basic peptides with partially higher hydrophobicity provided higher ACE inhibition activity than did neutral peptides. Finally, by using Q-TOF mass spectrometry, two peptide sequences (YPNQKV and FDIRA) with ACE inhibitory and antioxidative activities were successfully matched with a database. This study indicates that the WBS proteolysate can be a potential bifunctional food ingredient as the identified biopeptides demonstrated both ACE inhibitory and antioxidative activities in vitro.
    Matched MeSH terms: Angiotensin-Converting Enzyme Inhibitors/isolation & purification; Angiotensin-Converting Enzyme Inhibitors/chemistry*
  11. Effects of novel diarylpentanoid analogues of curcumin on secretory phospholipase A2 , cyclooxygenases, lipo-oxygenase, and microsomal prostaglandin E synthase-1
    Ahmad W, Kumolosasi E, Jantan I, Bukhari SN, Jasamai M
    Chem Biol Drug Des, 2014 Jun;83(6):670-81.
    PMID: 24406103 DOI: 10.1111/cbdd.12280
    Arachidonic acid and its metabolites have generated a heightened interest due to their significant role in inflammation. Inhibiting the enzymes involved in arachidonic acid metabolism has been considered as the synergistic anti-inflammatory effect. A series of novel curcumin diarylpentanoid analogues were synthesized and evaluated for their inhibitory effects on activity of secretory phospholipase A2 , cyclooxygenases, soybean lipo-oxygenase as well as microsomal prostaglandin E synthase-1. Among the curcumin analogues, compounds 3, 6, 9, 12, and 17 exhibited strong inhibition of secretory phospholipase A2 activity, with IC50 values ranging from 5.89 to 11.02 μm. Seven curcumin analogues 1, 3, 6, 7, 9, 11, and 12 showed inhibition of cyclooxygenases-2 with IC50 values in the range of 46.11 to 94.86 μm, which were lower than that of curcumin. Compounds 3, 6, 7, 12, and 17 showed strong inhibition of lipo-oxygenase enzyme activity. Preliminary screening of diarylpentanoid curcumin analogues for microsomal prostaglandin E synthase-1 activity revealed that four diarylpentanoid curcumin analogues 5, 6, 7, and 13 demonstrated higher inhibition of microsomal prostaglandin E synthase-1 activity with IC50 ranging from 2.41 to 4.48 μm, which was less than that of curcumin. The present results suggest that some of these diarylpentanoid analogues were able to inhibit the activity of these enzymes. This raises the possibility that diarylpentanoid analogues of curcumin might serve as useful starting point for the design of improved anti-inflammatory agents.
    Matched MeSH terms: Enzyme Inhibitors/pharmacology; Enzyme Inhibitors/chemistry
  12. Fulltext Novel angiotensin I-converting enzyme inhibitory peptides derived from an edible mushroom, Pleurotus cystidiosus O.K. Miller identified by LC-MS/MS
    Lau CC, Abdullah N, Shuib AS
    BMC Complement Altern Med, 2013 Nov 11;13:313.
    PMID: 24215325 DOI: 10.1186/1472-6882-13-313
    BACKGROUND: Angiotensin I-converting enzyme (ACE) inhibitors have been reported to reduce mortality in patients with hypertension. Compared to chemosynthetic drugs, ACE inhibitors derived from natural sources such as food proteins are believed to be safer for consumption and to have fewer adverse effects. Some edible mushrooms have been reported to significantly reduce blood pressure after oral administration. In addition, mushrooms are known to be rich in protein content. This makes them a potential source of ACE inhibitory peptides. Hence, the objective of the current study was to isolate and characterise ACE inhibitory peptides from an edible mushroom, Pleurotus cystidiosus.

    METHODS: ACE inhibitory proteins were isolated from P. cystidiosus based on the bioassay guided purification steps, i.e. ammonium sulphate precipitation, reverse phase high performance liquid chromatography and size exclusion chromatography. Active fraction was then analysed by LC-MS/MS and potential ACE inhibitory peptides identified were chemically synthesized. Effect of in vitro gastrointestinal digestions on the ACE inhibitory activity of the peptides and their inhibition patterns were evaluated.

    RESULTS: Two potential ACE inhibitory peptides, AHEPVK and GPSMR were identified from P. cystidiosus with molecular masses of 679.53 and 546.36 Da, respectively. Both peptides exhibited potentially high ACE inhibitory activity with IC50 values of 62.8 and 277.5 μM, respectively. SEC chromatograms and BIOPEP analysis of these peptides revealed that the peptide sequence of the hexapeptide, AHEPVK, was stable throughout gastrointestinal digestion. The pentapeptide, GPSMR, was hydrolysed after digestion and it was predicted to release a dipeptide ACE inhibitor, GP, from its precursor. The Lineweaver-Burk plot of AHEPVK showed that this potent and stable ACE inhibitor has a competitive inhibitory effect against ACE.

    CONCLUSION: The present study indicated that the peptides from P. cystidiosus could be potential ACE inhibitors. Although these peptides had lower ACE inhibitory activity compared to commercial antihypertensive drugs, they are derived from mushroom which could be easily obtained and should have no side effects. Further in vivo studies can be carried out to reveal the clear mechanism of ACE inhibition by these peptides.

    Matched MeSH terms: Angiotensin-Converting Enzyme Inhibitors/isolation & purification; Angiotensin-Converting Enzyme Inhibitors/chemistry*
  13. Extraction of antioxidative and antihypertensive bioactive peptides from Parkia speciosa seeds
    Siow HL, Gan CY
    Food Chem, 2013 Dec 15;141(4):3435-42.
    PMID: 23993504 DOI: 10.1016/j.foodchem.2013.06.030
    Antioxidative and antihypertensive bioactive peptides were successfully derived from Parkia speciosa seed using alcalase. The effects of temperature (25 and 50 °C), substrate-to-enzyme ratio (S/E ratio, 20 and 50), and incubation time (0.5, 1, 2 and 5h) were evaluated based on 2,2-diphenyl-1-picrylhydrazyl (DPPH), ferric reducing antioxidant power (FRAP) and angiotensin-converting enzyme (ACE) assays. Bioactive peptide extracted at a hydrolysis condition of: temperature=50 °C, S/E ratio=50 and incubation time=2h, exhibited the highest DPPH radical scavenging activity (2.9 mg GAE/g), reducing power (11.7 mM) and %ACE-inhibitory activity (80.2%). The sample was subsequently subjected to fractionation and the peptide fraction of <10 kDa showed the strongest bioactivities. A total of 29 peptide sequences from peptide fraction of <10 kDa were identified as the most potent contributors to the bioactivities. These novel bioactive peptides were suggested to be beneficial to nutraceutical and food industries.
    Matched MeSH terms: Angiotensin-Converting Enzyme Inhibitors/isolation & purification; Angiotensin-Converting Enzyme Inhibitors/chemistry*
  14. Fulltext Potent α-glucosidase and α-amylase inhibitory activities of standardized 50% ethanolic extracts and sinensetin from Orthosiphon stamineus Benth as anti-diabetic mechanism
    Mohamed EA, Siddiqui MJ, Ang LF, Sadikun A, Chan SH, Tan SC, et al.
    BMC Complement Altern Med, 2012;12:176.
    PMID: 23039079 DOI: 10.1186/1472-6882-12-176
    In the present study, we tested a 50% ethanolic extract of Orthosiphon stamineus plants and its isolated bioactive compound with respect to their α-glucosidase and α-amylase inhibitory activities.
    Matched MeSH terms: Enzyme Inhibitors/isolation & purification; Enzyme Inhibitors/pharmacology*
  15. In vitro modulatory effects of flavonoids on human cytochrome P450 2C8 (CYP2C8)
    Pang CY, Mak JW, Ismail R, Ong CE
    Naunyn Schmiedebergs Arch Pharmacol, 2012 May;385(5):495-502.
    PMID: 22307090 DOI: 10.1007/s00210-012-0731-5
    The inhibitory effects of five flavonoids with distinct chemical classes (flavones [luteolin], flavonols [quercetin and quercitrin], and flavanones [hesperetin and hespiridin]) on cDNA-expressed CYP2C8 were investigated. CYP2C8 was co-expressed with NADPH-cytochrome P450 reductase in Escherichia coli and used to characterise potency and mechanism of these flavonoids on the isoform. Tolbutamide 4-methylhydroxylase, a high-performance liquid chromatography-based assay, was selected as marker activity for CYP2C8. Our results indicated that the flavonoids inhibited CYP2C8 with different potency. The order of inhibitory activities was quercetin > luteolin > hesperetin > hesperidin > quercitrin. All of these compounds however exhibited mechanism-based inhibition. A number of structural factors were found to be important for inhibition; these include the molecular shape (volume to surface ratio), the number of hydroxyl groups as well as glycosylation of the hydroxyl group. Quercetin was the most potent inhibitor among the flavonoids examined in this study, and our data suggest that it should be examined for potential pharmacokinetic drug interactions pertaining to CYP2C8 substrates in vivo.
    Matched MeSH terms: Enzyme Inhibitors/pharmacology*; Enzyme Inhibitors/chemistry
  16. Fulltext Antioxidant, antimicrobial and tyrosinase inhibitory activities of xanthones isolated from Artocarpus obtusus F.M. Jarrett
    Hashim NM, Rahmani M, Ee GC, Sukari MA, Yahayu M, Amin MA, et al.
    Molecules, 2012;17(5):6071-82.
    PMID: 22614861 DOI: 10.3390/molecules17056071
    One of the most promising plants in biological screening test results of thirteen Artocarpus species was Artocarpus obtusus FM Jarrett and detailed phytochemical investigation of powdered dried bark of the plant has led to the isolation and identification of three xanthones; pyranocycloartobiloxanthone A (1), dihydroartoindonesianin C (2) and pyranocycloartobiloxanthone B (3). These compounds were screened for antioxidant, antimicrobial and tyrosinase inhibitory activities. Pyranocycloartobiloxanthone A (1) exhibited a strong free radical scavenger towards DPPH free radicals with IC50 value of 2 µg/mL with prominent discoloration observed in comparison with standard ascorbic acid, α-tocopherol and quercetin, The compound also exhibited antibacterial activity against methicillin resistant Staphylococcus aureus (ATCC3359) and Bacillus subtilis (clinically isolated) with inhibition zone of 20 and 12 mm, respectively. However the other two xanthones were found to be inactive. For the tyrosinase inhibitory activity, again compound (1) displayed strong activity comparable with the standard kojic acid.
    Matched MeSH terms: Enzyme Inhibitors/pharmacology*; Enzyme Inhibitors/chemistry
  17. Fulltext Bioactive compounds, antioxidant, xanthine oxidase inhibitory, tyrosinase inhibitory and anti-inflammatory activities of selected agro-industrial by-products
    Oskoueian E, Abdullah N, Hendra R, Karimi E
    Int J Mol Sci, 2011;12(12):8610-25.
    PMID: 22272095 DOI: 10.3390/ijms12128610
    Evaluation of abundantly available agro-industrial by-products for their bioactive compounds and biological activities is beneficial in particular for the food and pharmaceutical industries. In this study, rapeseed meal, cottonseed meal and soybean meal were investigated for the presence of bioactive compounds and antioxidant, anti-inflammatory, xanthine oxidase and tyrosinase inhibitory activities. Methanolic extracts of rapeseed meal showed significantly (P < 0.01) higher phenolics and flavonoids contents; and significantly (P < 0.01) higher DPPH and nitric oxide free radical scavenging activities when compared to that of cottonseed meal and soybean meal extracts. Ferric thiocyanate and thiobarbituric acid tests results showed rapeseed meal with the highest antioxidant activity (P < 0.01) followed by BHT, cotton seed meal and soybean meal. Rapeseed meal extract in xanthine oxidase and tyrosinase inhibitory assays showed the lowest IC(50) values followed by cottonseed and soybean meals. Anti-inflammatory assay using IFN-γ/LPS stimulated RAW 264.7 cells indicated rapeseed meal is a potent source of anti-inflammatory agent. Correlation analysis showed that phenolics and flavonoids were highly correlated to both antioxidant and anti-inflammatory activities. Rapeseed meal was found to be promising as a natural source of bioactive compounds with high antioxidant, anti-inflammatory, xanthine oxidase and tyrosinase inhibitory activities in contrast to cotton and soybean meals.
    Matched MeSH terms: Enzyme Inhibitors/analysis*; Enzyme Inhibitors/pharmacology
  18. alpha-Amylase inhibitory activity of some Malaysian plants used to treat diabetes; with particular reference to Phyllanthus amarus
    Ali H, Houghton PJ, Soumyanath A
    J Ethnopharmacol, 2006 Oct 11;107(3):449-55.
    PMID: 16678367
    Extracts of six selected Malaysian plants with a reputation of usefulness in treating diabetes were examined for alpha-amylase inhibition using an in vitro model. Inhibitory activity studied by two different protocols (with and without pre-incubation) showed that Phyllanthus amarus hexane extract had alpha-amylase inhibitory properties. Hexane and dichloromethane extracts of Anacardium occidentale, Lagerstroemia speciosa, Averrhoa bilimbiPithecellobium jiringa and Parkia speciosa were not active when tested without pre-incubation. Extraction and fractionation of Phyllanthus amarus hexane extract led to the isolation of dotriacontanyl docosanoate, triacontanol and a mixture of oleanolic acid and ursolic acid. Dotriacontanyl docosanoate and the mixture of oleanolic acid and ursolic acid are reported from this plant species for the first time. All compounds were tested in the alpha-amylase inhibition assay and the results revealed that the oleanolic acid and ursolic acid (2:1) mixture was a potent alpha-amylase inhibitor with IC(50)=2.01 microg/ml (4.41 microM) and that it contributes significantly to the alpha-amylase inhibition activity of the extract. Three pure pentacyclic triterpenoids, oleanolic acid, ursolic acid and lupeol were shown to inhibit alpha-amylase.
    Matched MeSH terms: Enzyme Inhibitors/pharmacology*; Enzyme Inhibitors/chemistry
  19. Coalesced chitosan activated carbon composite for batch and fixed-bed adsorption of cationic and anionic dyes
    Auta M, Hameed BH
    Colloids Surf B Biointerfaces, 2013 May 1;105:199-206.
    PMID: 23376092 DOI: 10.1016/j.colsurfb.2012.12.021
    A renewable waste tea activated carbon (WTAC) was coalesced with chitosan to form composite adsorbent used for waste water treatment. Adsorptive capacities of crosslinked chitosan beads (CCB) and its composite (WTAC-CCB) for Methylene blue dye (MB) and Acid blue 29 (AB29) were evaluated through batch and fixed-bed studies. Langmuir, Freundlich and Temkin adsorption isotherms were tested for the adsorption process and the experimental data were best fitted by Langmuir model and least by Freundlich model; the suitability of fitness was adjudged by the Chi-square (χ(2)) and Marquadt's percent standard deviation error functions. Judging by the values of χ(2), pseudo-second-order reaction model best described the adsorption process than pseudo-first-order kinetic model for MB/AB29 on both adsorbents. After five cycles of adsorbents desorption test, more than 50% WTAC-CCB adsorption efficiency was retained while CCB had <20% adsorption efficiency. The results of this study revealed that WTAC-CCB composite is a promising adsorbent for treatment of anionic and cationic dyes in effluent wastewaters.
    Matched MeSH terms: Enzyme Inhibitors/metabolism; Enzyme Inhibitors/chemistry*
  20. A Review of Bisindolylmethane as an Important Scaffold for Drug Discovery
    Imran S, Taha M, Ismail NH
    Curr Med Chem, 2015;22(38):4412-33.
    PMID: 26438249
    Bisindolylmethane and its derivatives are pharmacologically active and applicable in the field of pharmaceutical chemistry. Bisindolylmethanes have a variety of biological activities such as antihyperglycemic, antiinflammatory, antibacterial, anticancer, and antileishmanial activities, including enzyme inhibition activity. They play a crucial role in many diseases especially anticancer activity. Modifying their structure had proven to be useful in the search of new therapeutic agents. Extensive research carried out on bisindolylmethane and its derivatives shows that they are pharmacologically significant. The present review focuses on the pharmacological profile of bisindolylmethane derivatives. This review includes the current literature with an update of research findings as well as the perspectives that they hold for future research.
    Matched MeSH terms: Enzyme Inhibitors/pharmacology; Enzyme Inhibitors/chemistry*
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