Effect of Yoganidra on Blood Pressure, Hs-CRP, and Lipid Profile of Hypertensive Subjects: A Pilot Study.

BACKGROUND: Yoganidra is a systematic method of promoting a state of complete physical, mental, and emotional relaxation. It is a safe, inexpensive, and very effective method of management of hypertension when used along with standard pharmacological therapy. This study aims to assess the effect of yoganidra on blood pressure (both systolic blood pressure (SBP) and diastolic blood pressure (DBP)), Hs-CRP, and lipid profile of hypertensive subjects at the time of enrollment (subjects that are hypertensive at the time of enrollment). METHODS: Both treated and untreated subjects (n = 74) with hypertension (blood pressure ≥140/90 mmHg) and age between 35 and 70 years were included in this study after obtaining ICMR-NIN-IEC approval and written informed consent from all subjects. Subjects with critical illness and/or psychological disturbances were excluded from this study. The subjects in the experimental group (n = 31) practiced yoganidra for 45 minutes daily for 12 weeks under strict supervision. There was no intervention in the control group (n = 43). Weekly blood pressure was recorded in the experimental group, whereas it was performed at baseline and at endpoint for control groups. Hs-CRP and lipid profile were estimated at baseline and endpoint for both the groups. RESULTS: A significant reduction in mean SBP from 142.9 mm Hg (SD ± 16.46) to 118.68 mm Hg (SD ± 9.21; p value 0.0001) and DBP from 89.84 mm Hg (SD ± 10.42) to 77.03 mm Hg (SD ± 6.47: p value 0.0001) was observed among the experimental group after 12 weeks of yoganidra practice when compared with the control group. A significant reduction in mean Hs-CRP (2.21 ± 1.49 to 1.06 ± 0.82 mg/L, p < 0.001 ∗∗∗ ) was observed among the experimental group. There were no significant differences between triglycerides and total cholesterol levels, whereas LDL-C and HDL-C showed a trend of improvement in the experimental group after intervention. CONCLUSIONS: In this pilot study, we observed a significant reduction in blood pressure and Hs-CRP in the yoganidra group compared with the control group. There were no significant side effects observed in the intervention group during the study period.

Rapid detection of DPP-IV activity in porcine serum: A fluorospectrometric assay.

Dipeptidyl peptidase IV (DPP-IV) is an aminopeptidase that cleaves the N-terminal dipeptide from peptides bearing proline or alanine residues. Currently, DPP-IV activity is quantified by spectrophotometric or fluorometric methods, which employ Gly-Pro-pNA and Gly-Pro-AMC respectively, as substrate. However, these methods require high enzyme and substrate concentrations. In this study, we adapted the DPP-IV fluorospectrometric assay using NanoDrop 3300, which requires only nanogram levels of the enzyme (30 ng crude DPP-IV) and considerably low substrate concentrations (100 µM). Fluorescence measurement required a reaction mixture of only 2 µL, thus eliminating the need for microtiter plates or cuvettes.We employed this assay to demonstrate DPP-IV activity in porcine serum for the first time. The enzymatic activity peaked at pH 8.0 in porcine (84 nM/min), human (87 nM/min) and bovine (89.1 nM/min) sera, with the optimum temperature of 37 °C. The enzyme showed maximum activity upon incubation for 40 min at 37 °C. In contrast, activity in the porcine serum was the highest after incubation for 30 min at the same optimized parameters. The IC50 values of diprotin A against DPP-IV from human, porcine, and bovine sera were 7.83, 8.62, 9.17 µM, respectively. The present assay procedure is a convenient, sensitive, accurate and high-throughput method suitable for primary screening of DPP-IV inhibitors.

Procoagulant serine glycoprotease from Cucumis sativus L.: action on human fibrinogen and fibrin clot.

Upon examination of the fruit extract of Cucumis sativus L. for its pharmacological benefits, it was previously observed that it has potential proteolytic, fibrinogenolytic and procoagulant activities. These properties can be attributed to the presence of the protease. In this regard, the present study comprised of purification and characterization of protease. Purification of the enzyme involved ammonium sulfate precipitation followed by gel filtration and ion exchange chromatography. The purified cucumis protease (CPro) exhibits homogeneity as attested by SDS-PAGE and RP-HPLC with a retention time of 14.246 min with molecular mass ~75.3 kDa. CPro was identified as a glycoprotein and serine protease. Azocasein is the preferred substrate for CPro as it showed low Km value of 0.3809 mg/ml. Purified CPro exhibits optimum activity at 37 °C and pH 8. CPro shows its involvement in hemostasis-the very first step in wound healing. CPro degrades the subunits of human fibrinogen in the order Aα > Bß > Î³. It also hydrolyzes the subunits of the partially cross-linked fibrin clot in the order α-polymer > Î³-γ dimer > ß-chain. CPro reduced the clotting time of citrated plasma, prothrombin time and activated partial thromboplastin time of plasma. CPro is neither hemorrhagic nor edema-inducing, thus considered to be a non-toxic protease. This work provides evidence for the use of cucumber extract in wound healing and authenticates its use in cosmetics.

Exploring hemostatic and thrombolytic potential of heynein - A cysteine protease from Ervatamia heyneana latex.

ETHNOPHARMACOLOGICAL RELEVANCE: The latex of Ervatamia heyneana (Wall.) T. Cooke plant has been used for wound healing and various skin diseases by Indian tribes and folklore. AIM OF THE STUDY: To validate the scientific basis of heynein - a key protease of Ervatamia heyneana, in hemostasis and wound healing process. MATERIALS AND METHODS: The latex from E. heyneana was processed and subjected to two step purification. The purified heynein was assayed for proteolytic activity using casein as substrate and also attested by zymography. The inhibition studies confirmed the nature of heynein. Pure fibrinogen was used for fibrinogenolytic activity and citrated plasma was used for coagulant and fibrinolytic activities. The edema inducing action and hemorrhagic activity of heynein were assessed on mice model. RESULTS: The purified heynein exhibited proteolytic activity, which was confirmed by caseinolytic assay and zymography. The inhibition studies confirmed heynein to be a cysteine protease. Heynein showed complete hydrolysis of all the three subunits of human fibrinogen (Aα, Bß, γ). It exhibited strong pro-coagulant activity by reducing plasma clotting time from 248 to 39s at 40µg concentration. Heynein cleaved α polymer subunit in fibrin clot and did not induce edema and hemorrhage in mice models. The non-hemorrhagic nature was supported with histopathological studies of skin samples. CONCLUSION: Heynein displays strong pro-coagulant action associated with fibrin(ogen)olytic activity. This provides basis for the observed pharmacological action of Ervatamia heyneana and thereby justifies its use in folk medicine.

Caralluma umbellata Peroxidase: Biochemical Characterization and Its Detoxification Potentials in Comparison with Horseradish Peroxidase.

Caralluma umbellata peroxidase (CUP) is an acidic heme-containing protein having a molecular weight of ~42 kDa and is specific to guaiacol. It is not a glycoprotein. It was purified to 12.5-fold purity with 6.16 % yield. Its activity is dependent on hydrogen peroxide and has an optimum pH and temperature of 6.2 and 45 °C respectively. It can decolorize dyes, viz., Aniline Blue, Reactive Black 5, and Reactive Blue 19 but not Congo Red, while HRP can decolorize Congo Red also. It has lignin-degrading potentiality as it can decompose veratryl alcohol. Detoxification of phenol was more by CUP compared to HRP while with p-nitrophenol HRP has a greater detoxification rate. Based on our results, CUP was identified to be capable of oxidizing a variety of hazardous substances and also a lignin-degrading plant biocatalyst.

Purification and characterization of novel fibrin(ogen)olytic protease from Curcuma aromatica Salisb.: Role in hemostasis.

BACKGROUND: The proteases from turmeric species have procoagulant and fibrinogenolytic activity. This provides a scientific basis for traditional use of turmeric to stop bleeding and promote wound healing processes. PURPOSE: Our previous studies revealed that fibrinogenolytic action of crude enzyme fraction of Curcuma aromatica Salisb., was found to be more influential than those of Curcuma longa L., Curcuma caesia Roxb., Curcuma amada Roxb. and Curcuma zedoria (Christm.) Roscoe. Hence, the purpose of this study is to purify and characterize protease from C. aromatica and to explore its role in wound healing process. METHODS: The protease was purified by Sephadex G-50 gel permeation chromatography. Peak with potent proteolytic activity was subjected to rechromatography and then checked for homogeneity by SDS-PAGE and native PAGE. Furthermore purity of the peak was assessed by RP-HPLC and MALDI-TOF. The biochemical properties, type of protease, kinetic studies, fibrinogenolytic, coagulant and fibrinolytic activities were carried out. RESULTS: The two proteolytic peaks were fractionated in gel permeation chromatography. Among these, the peak-II showed potent proteolytic activity with specific activity of 10units/mg/min and named as C. aromatica protease-II (CAP-II). This protein resolved into a single sharp band both in SDS-PAGE (reducing and non-reducing) as well as in native (acidic) PAGE. It is a monomeric protein, showing sharp peak in RP-HPLC and its relative molecular mass was found to be 12.378kDa. The caseinolytic and fibrinolytic activity of CAP-II was completely inhibited by phenylmethylsulfonylfluoride (PMSF). The CAP-II exhibited optimum temperature of 45°C and optimum pH of 7.5. The Km and Vmax of CAP-II was found to be 1.616µg and 1.62units/mg/min respectively. The CAP-II showed hydrolysis of all three subunits of fibrinogen in the order Aα>Bß>γ. The CAP-II exhibited strong procoagulant activity by reducing the human plasma clotting time. It also showed fibrinolytic activity by complete hydrolysis of α-polymer and γ-γ dimer present in fibrin. CONCLUSION: The CAP-II is a novel serine protease from C. aromatica, which has been demonstrated to stop bleeding and initiate wound healing through its procoagulant and fibrin(ogen)olytic activities. Our study demonstrates the possible role of CAP-II, as therapeutic enzyme to stop bleeding at the time of wounding.

Comparative analysis of procoagulant and fibrinogenolytic activity of crude protease fractions of turmeric species.

ETHNAOPHARMACOLOGIAL RELEVANCE: Turmeric rhizome is a traditional herbal medicine, which has been widely used as a remedy to stop bleeding on fresh cuts and for wound healing by the rural and tribal population of India. AIM OF THE STUDY: To validate scientific and therapeutic application of turmeric rhizomes to stop bleeding on fresh cuts and its role in wound healing process. MATERIALS AND METHODS: The water extracts of thoroughly scrubbed and washed turmeric rhizomes viz., Curcuma aromatica Salisb., Curcuma longa L., Curcuma caesia Roxb., Curcuma amada Roxb. and Curcuma zedoria (Christm.) Roscoe. were subjected to salting out and dialysis. The dialyzed crude enzyme fractions (CEFs) were assessed for proteolytic activity using casein as substrate and were also confirmed by caseinolytic zymography. Its coagulant activity and fibrinogenolytic activity were assessed using human citrated plasma and fibrinogen, respectively. The type of protease(s) in CEFs was confirmed by inhibition studies using specific protease inhibitors. RESULTS: The CEFs of C. aromatica, C. longa and C. caesia showed 1.89, 1.21 and 1.07 folds higher proteolytic activity, respectively, compared to papain. In contrast to these, C. amada and C. zedoria exhibited moderate proteolytic activity. CEFs showed low proteolytic activities compared to trypsin. The proteolytic activities of CEFs were confirmed by caseinolytic zymography. The CEFs of C. aromatica, C. longa and C. caesia showed complete hydrolysis of Aα, Bß and γ subunits of human fibrinogen, while C. amada and C. zedoria showed partial hydrolysis. The CEFs viz., C. aromatica, C. longa, C. caesia, C. amada and C. zedoria exhibited strong procoagulant activity by reducing the human plasma clotting time from 172s (Control) to 66s, 84s 88s, 78s and 90s, respectively. The proteolytic activity of C. aromatica, C. longa, C. caesia and C. amada was inhibited (>82%) by PMSF, suggesting the possible presence of a serine protease(s). However, C. zedoria showed significant inhibition (60%) against IAA and moderate inhibition (30%) against PMSF, indicating the presence of cysteine and serine protease(s). CONCLUSION: The CEFs of turmeric species exhibited strong procoagulant activity associated with fibrinogenolytic activity. This study provides the scientific credence to turmeric in its propensity to stop bleeding and wound healing process practiced by traditional Indian medicine.

Exploring a new serine protease from Cucumis sativus L.

Coagulation is an important physiological process in hemostasis which is activated by sequential action of proteases. This study aims to understand the involvement of aqueous fruit extract of Cucumis sativus L. (AqFEC) European burp less variety in blood coagulation cascade. AqFEC hydrolyzed casein in a dose-dependent manner. The presence of protease activity was further confirmed by casein zymography which revealed the possible presence of two high molecular weight protease(s). The proteolytic activity was inhibited only by phenyl methyl sulphonyl fluoride suggesting the presence of serine protease(s). In a dose-dependent manner, AqFEC also hydrolysed Aα and Bß subunits of fibrinogen, whereas it failed to degrade the γ subunit of fibrinogen even at a concentration as high as 100 µg and incubation time up to 4 h. AqFEC reduced the clotting time of citrated plasma by 87.65%. The protease and fibrinogenolytic activity of AqFEC suggests its possible role in stopping the bleeding and ensuing wound healing process.

Synergistic Caseinolytic Activity and Differential Fibrinogenolytic Action of Multiple Proteases of Maclura spinosa (Roxb. ex Willd.) latex.

BACKGROUND: Kollamalayaali tribes of South India use latex of Maclura spinosa for milk curdling. This action is implicated to proteases which exhibit strong pharmacological potential in retardation of blood flow and acceleration of wound healing. OBJECTIVE: To validate the presence of a proteolytic enzyme(s) in Maclura spinosa latex (MSL), and to investigate their probable role in hemostasis. MATERIALS AND METHODS: Processed latex was examined for proteolytic and hemostatic activity using casein and human fibrinogen as substrates, respectively. Caseinoltyic activity was compared with two standard proteases viz., trypsin I and trypsin II. Effect of various standard protease inhibitors viz., iodoacetic acid (IAA), phenylmethylsulfonyl fluoride (PMSF), ethylene glycol tetraacetic acid, and ethylenediaminetetraacetic acid on both caseinolytic and fibrinogenolytic activities were examined. Electrophoretogram of fibrinogenolytic assays were subjected to densitometric analysis. RESULTS: Proteolytic action of MSL was found to be highly efficient over trypsin I and trypsin II in dose-dependent caseinolytic activity (P < 0.05; specific activity of 1,080 units/mg protein). The Aα and Bß bands of human fibrinogen were readily cleaved by MSL (for 1 µg crude protein and 30 min of incubation time). Furthermore, MSL cleaved γ subunit in dose- and time-dependent manner. Quantitative correlation of these results was obtained by densitometric analysis. The caseinolytic activity of MSL was inhibited by IAA, PMSF. While, only PMSF inhibited fibrinogenolytic activity. CONCLUSIONS: MSL contains proteolytic enzymes belonging to two distinct superfamilies viz., serine protease and cysteine proteases. The fibrinogenolytic activity of MSL is restricted to serine proteases only. The study extrapolates the use of M. spinosa latex from milk curdling to hemostasis. SUMMARY: Proteolytic enzymes present in latex of Maclura spinosa can be assigned to two different protease superfamilies viz., serine protease and cysteine protease as revealed by the inhibitory studies of caseinolytic activity. Among them, only serine protease can be considered as hemostatically significant as inhibition of fibrinogenolytic action of Maclura spinosa latex protease is shown only by PMSF, a serine protease-specific inhibitor. Abbreviations used: MSL: Maclura spinos Latex, IAA: Iodo Acetic Acid, EDTA: Ethylene Diamine Tetra Acetic Acid, EGTA: Ethylene glycol tetra acetic acid, PMSF: Phenyl methyl sulphonyl fluoride.

Evidence for peroxidase activity in Caralluma umbellata.

Vast applications of peroxidases create an increasing demand to characterize peroxidases from new sources with more applicability potential. The aim of the present study was to check the presence of peroxidase activity from Caralluma umbellata. This is the first report on the C. umbellata peroxidase (CUP). The presence of peroxidase was revealed by the histochemical analysis of the stem sections, zymographic studies, and in vitro peroxidase activity assay using various reducing substrates viz., 2, 2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) (ABTS), guaiacol, o-dianisidine, and ferulic acid. The band pattern in zymogram confirms that CUP has a molecular weight less than that of horseradish peroxidase (44 kDa). Comparative evaluation of peroxidase activity of CUP with respect to horseradish peroxidase (HRP) indicates that CUP catalyzes ABTS and ferulic acid in a similar pattern as HRP but with guaiacol, the extent of catalysis shown by CUP over HRP is high. The standard inhibitors sodium azide and sodium meta bisulphite inhibited CUP activity in a dose dependent manner.

1-(3-Bromo-2-thien-yl)ethanone.

In the title compound, C(6)H(5)BrOS, the non-H and aromatic H atoms lie on a crystallographic mirror plane. In the crystal, mol-ecules are linked into chains propagating along the c axis by inter-molecular C-H⋯O hydrogen bonds.

N-[4-Cyano-3-(trifluoro-meth-yl)phen-yl]-2-meth-oxy-benzamide.

In the title compound, C(16)H(11)F(3)N(2)O(2), the carboxamide group connecting the two aromatic rings is in a syn-periplanar configuration; the mol-ecule is non-planar; the dihedral angle between the two aromatic rings is 13.95 (18)°. Intra-molecular N-H⋯O and C-H⋯O hydrogen bonds occur. In the crystal, mol-ecules are linked by inter-molecular C-H⋯O hydrogen bonds.

Synthesis, characterization and in vitro anti-tumor activities of novel 9-ethyl-9H-purine derivatives.

Newer series of 9-ethyl-9H-purine derivatives (EPD) were synthesized and screened for their efficacy in inhibiting the proliferation of various tumor cells in vitro. We evaluated the effects of EPD against HeLa, SiHa, CaSki (human cervical cancer cells), LM8, LM8G7 (murine osteosarcoma cells), OVSAHO and SKOV-3 (human ovarian cancer cells). The chemical structures of the EPD were confirmed by (1)H NMR and LCMS analyses. The inhibitory effects of EPD were studied by using trypan blue exclusion, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) and TetraColor One reagents. Furthermore, SAR studies revealed that the presence of trifluoromethoxy and trifluromethyl group in 4b and 4g, respectively are responsible for the significant activity of the EPD against cervical cancer cells and the presence of isopropoxy group in 4f has influence in inhibiting the proliferation of osteosarcoma and ovarian cancer cell types.

Chemistry and structural evaluation of different phospholipase A2 inhibitors in arachidonic acid pathway mediated inflammation and snake venom toxicity.

PLA2 inhibitors specific to Group I and II PLA2 isoforms are therapeutically important as anti-inflammatory molecules and against venom toxicity. From various natural sources diversified molecules with PLA2 inhibition and concomitant neutralization of inflammatory reactions and venom toxicity were characterized. Using these molecules, lead compounds are generated in several laboratories. Analogues of lead molecules were generated by substituting different types of functional groups in order to obtain a molecule with optimal PLA2 inhibition. The lead molecules characterized as PLA2 inhibitors are indoles, azetidinones, piperazines, isoxazolidines, isoxazolines, diazepinones, acenaphthenes and several substrate analogues. The lead optimization involves relative hydrophobicity and substitution of functional groups, such as electron withdrawing or donating. Many such groups are placed on hydrophobic moiety and their positional bioisosters are characterized. Among these analogue piperazine derivatives on optimization with respect to hydrophobicity and electronegativity showed inhibition at nanomolar levels. Structural analysis of many lead molecules indicated that a PLA2 inhibitor should have both hydrophobic moiety and polar functional groups. Each lead molecule requires optimization in this regard for effective inhibition.

2-(2-(2-Ethoxybenzoylamino)-4-chlorophenoxy)-N-(2-ethoxybenzoyl)benzamine inhibits EAT cell induced angiogenesis by down regulation of VEGF secretion.

Compounds containing amide bond play a pivotal role in various pharmaceutical applications. 2-(2-(2-Ethoxybenzoylamino)-4-chlorophenoxy)-N-(2-ethoxybenzoyl)benzamine 4 is shown to be a potent antiangiogenic agent. In this study, we report the microwave-assisted synthesis, single crystal X-ray structure, and antiangiogenic effect of compound 4 in EAT cell induced angiogenesis. Treatment with compound 4 in vivo demonstrated down regulation of the secretion of VEGF in EAT cells and inhibition of blood vessel formation indicating the potential angioinhibitory effect of the compound in EAT cells.

Synthesis, characterization, antimicrobial and single crystal X-ray crystallographic studies of some new sulfonyl, 4-chloro phenoxy benzene and dibenzoazepine substituted benzamides.

A new class of benzamide derivatives 3a(I-VI) and 3b(I-VI), bearing different bioactive moieties were synthesized and evaluated for their efficacy as antimicrobials in vitro. Compounds 3bVI, 3aII, 3aV, 3bIII, 3aVI, 3bII showed significant antibacterial activity and 3bIII, 3bII, 3aIV, 3bV, 3bVI, 3aI exhibit significant antifungal activity. The title compounds are characterized by spectral and elemental analysis. Compounds 2-methoxy-N-[4-(thiazol-2-yl-sulfamoyl)-phenyl]-benzamide 3aII and 2-(2-(2-ethoxybenzoylamino) phenethyl)-N-(2-ethoxybenzoyl) benzenamine 3bV are characterized by the single crystal X-ray studies. Compound 3aII crystallizes in monoclinic space group P2(1) and 3bV in triclinic space group P-1. Compounds 3aII and 3bV exhibit both inter and intra molecular hydrogen bonding.

Synthesis of pharmaceutically important condensed heterocyclic 4,6-disubstituted-1,2,4-triazolo-1,3,4-thiadiazole derivatives as antimicrobials.

The two series of 4,6-disubstituted 1,2,4-triazolo-1,3,4-thiadiazole derivatives 2(a-e) and 3(a-e) were synthesized and characterized using IR, (1)H-NMR, CHNS analysis and by single crystal X-ray crystallographic studies. The compound 6-(2-chloro-phenyl)-3-ethyl-[1,2,4]triazole[3,4-b]thiadiazole 2b has been characterized by single crystal X-ray diffraction method. The compound crystallizes in monoclinic space group P2(1)/c with a cell parameters a = 11.879(1) Angstroms, b = 15.112(2) Angstroms, c = 13.95(2) Angstroms, Z = 8 and the final R factor is R1= 0.0524. The structure exhibits both intra and intermolecular hydrogen bonds. The title compounds were checked for their efficacy as antimicrobials in vitro. Compounds 2b, 2c, 2d, 3b, 3c and 3d showed significant inhibition against all the strains tested, when compared to standard drugs.

Microwave-assisted synthesis of N-alkylated benzotriazole derivatives: antimicrobial studies.

Synthesis and characterization of N-alkylated benzotriazole derivatives 2(a-g) bearing pharmaceutically important bioactive substituents and their antimicrobial studies in vitro are described. The syntheses of the compounds were achieved by N-alkylation of the benzotriazole with different bioactive alkyl halides in presence of powdered K2CO3 in DMF solution and by microwave irradiation method with good yield compared to conventional method. The crystal structure analysis shows that compound 4'-benzotriazol-1-yl-methyl-biphenyl-2-carbonitrile 2a crystallizes in the space group P1 with cell parameters a = 8.526 (3) A, b = 12.706 (3) A, c = 7.966 (2) A, alpha = 100.89 (2) degrees , beta = 101.63 (3) degrees , gamma = 102.20(2) degrees, Volume = 801.7(4) A degrees , Z = 2 and the final R factor is 0.0559 for 6130 reflections with 218 parameters and zero restraint. This structure exhibits intermolecular hydrogen bonding. Compounds 2e, 2a showed significant antimicrobial activity.

Synthesis and characterization of novel 6-fluoro-4-piperidinyl-1,2-benzisoxazole amides and 6-fluoro-chroman-2-carboxamides: antimicrobial studies.

Novel derivatives of 6-fluoro-4-piperidinyl-1,2-benzisoxazole amides 4(I-VI) were obtained by the condensation of different acid chlorides with 6-fluoro-3-piperidin-4yl-benzo[d]isoxazole. Also, 6-fluoro-chroman-2-carboxamides 6(I-III) were synthesized by using nebulic acid chloride with different amines in presence of triethylamine as acid scavenger and dichloroethane as solvent. The synthesized compounds were characterized by IR, 1H NMR, and CHN analysis. These molecules were evaluated for their efficacy as antimicrobials in vitro by disc diffusion and microdilution method against pathogenic strains such as Bacillus substilis, Escherichia coli, Pseudomonas fluorescens, Xanthomonas campestris pvs, X. oryzae, Aspergillus niger, A. flavus, Fusarium oxysporum, Trichoderma species, F. monaliforme, and Penicillum species. Compounds 4I, 4IV, 4V, 6I, 6II and 6III showed better inhibitory activity than compared to standard drugs. Among these compounds, 4IV and 6III showed potent inhibitory activity against all the strains and found to be nonstrain dependent. The title compounds represent a novel class of potent antimicrobial agents.