• Title/Summary/Keyword: Membrane binding

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Biorational Screening System Using Cyanobacteria(Anacystis nidulans $R_2$) for Searching the Photosynthetic Electron Transport Inhibitors (Cyanobacteria를 이용한 광합성 전자전달저해제의 생합리적 스크리닝)

  • Hwang, I.T.;Hong, K.S.;Cho, K.Y.;Yoshida, S.
    • Korean Journal of Weed Science
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    • v.13 no.2
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    • pp.81-88
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    • 1993
  • For searching the photosynthetic electron transport(PET) inhibitors, bio-rational screening system using thylakoid membranes extracted from wild and mutant cyanobacteria(Anacystis nidulans $R_2$) was developed. Generally, thylakoid membrane was more sensitive to the tested herbicides than the chloroplast from spinach in the Hill reaction. Higher resistant characteristics appeared in mutant D-5, Di-22 to diuron and mutant G-264 to atrazine as compared to wild type. To test the reaction of thylakoid membrane to herbicides, diuron and atrazine were applied simultaneously. Diuron and atrazine competed each other for binding with substituted amino acids, while diuron and dinoseb were non-competitive, and inhibiting activity was increased. Conclusively, bio-rational screening system using cyanobacteria was proved to be fast and efficient screening method for the development of PET inhibitors.

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Ultrastnlctural changes of Acanthamoeba cyst of clinical isolates after treatment with minimal cysticidal concentration of polyhexamethylene biguanide (최저살충농도의 PHMB로 처리한 각막염 유래 가시아메바 세포 미세구조 변화의 투과전자현미경적 관찰)

  • 공현희;정동일
    • Parasites, Hosts and Diseases
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    • v.36 no.1
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    • pp.7-14
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    • 1998
  • In order to understand the action mechanism of polyhexamethylene biguanide (PHMB) to the cyst of Accnthcnloebc on the morphological basis, the cysts of four corneal isolates of Acanthanoebc were treated with minimal cysticidal concentration (MCC) of PHMB and their ultrastructural changes were examined by transmission electron microscopy. The most striking change of cysts treated with PHMB compared with normal cysts was the shrinkage of intracystic amoebae, which resulted in the separation of the plasma membrane of intracystic amoeba from endocystic wall. Subplasmalemmal lipid droplets became irregularly shaped . In severely damaged cysts, cytoplasm was aggregated and organelles were severely deformed. Cytoplasmic materials were leaked out through the damaged plasma membrane. Most cysts showed aggregation of nuclear chromatin material. Number of mitochondrial cristae was also reduced. Ecto- and endo-cystic walls were relatively well tolerated. Findings in the present study revealed that PHMB affected mainly on plasma membrane, but lesser on organellar membrane of intracystic amoeba. It seemed likely that PHMB might kill cystic forms of Accnthamoebc by similar mechanism in which this environmental biocide can damage the cell wall of Escherichia coli by binding with acidic phospholipids.

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Effects of Bacillus thuringiensis ${\delta}$-Endotoxin on Insect Fat Body Structure

  • Cheon, Hyang-Mi;Kim, Hong-Ja;Gang, Seok-Won;Seo, Suk-Jae
    • Animal cells and systems
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    • v.1 no.3
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    • pp.507-513
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    • 1997
  • Sequential observations of binding patterns and structural effects of Bacillus thuringiensis var. kurstaki were made on fat body tissue of the fall webworm, Hyphantria cunea Drury. Fat body was cultured in vitro in the presence of purified 62 kDa endotoxin and then examined for protein synthesis and the localization of membrane-bound toxin detected by an antibody against the 62 kDa endotoxin. Protein synthesis was mostly inhibited at concentrations of 15 ${\mu}$g/ml and higher. Immunocytochemical observations suggest that the toxin binds to all exposed basal lamina surrounding the fat body without apparent specificity. The cytopathic effect delectable by scanning electron microscope is disintegration rather than cell swelling. The basal lamina bound toxin was eventually detached from the fat body and followed by an extrusion of cell contents like lipid granules.

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Regulatgion of the Transport of Vitellogenin by Heterotrimeric G-Proteins during Oogenesis of a Polychaete, Pseudopotamilla occelata

  • Yi, Bong-Kyung;Lee, Yang-Rim
    • Animal cells and systems
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    • v.2 no.1
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    • pp.93-97
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    • 1998
  • Coelomoic fluid protein (CP), a vitellogenin contained in the coelomic fluid of polychaetes, is transported by receptor-mediated endocvtosis that is controlled by GTP-binding proteins. Transport of 125l-CP was markedly inhibited by AlF4 and toxins such as cholera toxin and pertussis toxin. These effects appear to be mediated by cAMP, since 125l-CP transport was also greatly inhibited by dibutyryl cAMP. The results strongly suggest that hetero trimeric G-protein is involved in the regulation of 125l=CP transport through the activation of adenylyl cyclase. Immunoblotting tests with antibodies against Gsa and Gia subunits showed a Gsa subunit of 45 kDa in the membrane of oocytes of intermediate and large size classes and a Gia subunit of 41 kDa only in the oocytes of the intermediate size class.

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A Solid-state NMR Study of the Kinetics of the Activity of an Antimicrobial Peptide, PG-1 on Lipid Membranes

  • Kim, Chul;Wi, Sungsool
    • Bulletin of the Korean Chemical Society
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    • v.33 no.2
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    • pp.426-432
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    • 2012
  • The activity of an antimicrobial peptide, protegrin-1 (PG-1), on lipid membranes was investigated using solidstate NMR and a new sampling method that employed mechanically aligned bilayers between thin glass plates. At 95% hydration and full hydration, the peptide respectively disrupted 25% and 86% of the aligned 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphotidylcholine (POPC) bilayers at a P/L (peptide-to-lipid) ratio of 1/20 under the new experimental conditions. The kinetics of the POPC bilayers disruption appeared to be diffusioncontrolled. The presence of cholesterol at 95% hydration and full hydration reduced the peptide disruption of the aligned POPC bilayers to less than 10% and 35%, respectively. A comparison of the equilibrium states of heterogeneously and homogeneously mixed peptides and lipids demonstrated the importance of peptide binding to the biomembrane for whole membrane disruption.

Enhancing Activity of Anticancer Drugs in Multidrug Resistant Tumors by Modulating P-Glycoprotein through Dietary Nutraceuticals

  • Khan, Muhammad;Maryam, Amara;Mehmood, Tahir;Zhang, Yaofang;Ma, Tonghui
    • Asian Pacific Journal of Cancer Prevention
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    • v.16 no.16
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    • pp.6831-6839
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    • 2015
  • Multidrug resistance is a principal mechanism by which tumors become resistant to structurally and functionally unrelated anticancer drugs. Resistance to chemotherapy has been correlated with overexpression of p-glycoprotein (p-gp), a member of the ATP-binding cassette (ABC) superfamily of membrane transporters. P-gp mediates resistance to a broad-spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively expelling the drugs from cells. Use of specific inhibitors/blocker of p-gp in combination with clinically important anticancer drugs has emerged as a new paradigm for overcoming multidrug resistance. The aim of this paper is to review p-gp regulation by dietary nutraceuticals and to correlate this dietary nutraceutical induced-modulation of p-gp with activity of anticancer drugs.

A New Cyclophilin Inhibitor from Ganoderma lucidum: Purification and Characterization

  • Lim, Jin-Ik;Jeong, Ki-Chul;Kang, In-Sug;Kim, Soo-Ja
    • Bulletin of the Korean Chemical Society
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    • v.25 no.7
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    • pp.1055-1060
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    • 2004
  • A new inhibitor for peptidylprolyl cis-trans isomerase (PPIase) has been isolated from Ganoderma lucidum and purified to homogeneous state by organic solvent extraction. The purified PPIase inhibitor (GPI) is assumed to be a membrane-associated glycoprotein. GPI inhibits specifically the bovine brain PPIase, a cyclophilin, and has no effect on the FKBP activity. The results of our chemical modification study of GPI indicate the presence of Lys residue(s) at or near its binding site. Like CsA-cyclophilin complex, GPI-bovine brain PPIase complex strongly inhibits the calcineurin activity in vitro, suggesting the possible involvement of GPI in immunomodulating pathway by the formation of PPIase-inhibitor-calcineurin complex.

Tertiary Structure of PreSl(21-47) of Hepatitis B Virus Studied by NMR Spectroscopy

  • Kyeunghee Yu;Cho, Eun-Wie;Shin, Song-Yub;Kim, Kol-Lyong;Kim, Yangmee
    • Journal of the Korean Magnetic Resonance Society
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    • v.4 no.1
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    • pp.41-49
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    • 2000
  • To design more efficient peptide antagonist against the HBV, preSl(21-47) which carries the HBV receptor binding site for hepatocytes was synthesized and the solution structure of preSl(21-47) was investigated using CD spectroscopy and NMR spectroscopy in membrane-mimicking environments. According to CD spectra, preSl(21-47) has a random structure in aqueous solution, while conformational change was induced by addition of TFE and SDS micelle. Tertiary structures as determined by NMR spectroscopy shows that preSl(21-47) has a very flexible structure even in SDS micelle.

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Swapping of interaction partners with ATG5 for autophagosome maturation

  • Kim, Jun Hoe;Song, Hyun Kyu
    • BMB Reports
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    • v.48 no.3
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    • pp.129-130
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    • 2015
  • Autophagy is a tightly regulated lysosome-mediated catabolic process in eukaryotes that maintains cellular homeostasis. A distinguishable feature of autophagy is the formation of double- membrane structures, autophagosome, which envelopes the intracellular cargoes and finally degrades them by fusion with lysosomes. So far, many structures of Atg proteins working on the autophagosome formation have been reported, however those involved in autophagosome maturation, a fusion with lysosome, are relatively unknown. One of the molecules in autophagosome maturation, TECPR1, has been identified and recently, structural studies on both ATG5-TECPR1 and ATG5-ATG16L1 complexes revealed that TECPR1 and ATG16L1 share the same binding site on ATG5. These results, in combination with supporting biochemical and cellular biological data, provide an insight into a model for swapping ATG5 partners for autophagosome maturation.

Cloning and expression of human $\beta$$_2$-adrenergic receptor in Saccharomyces cerevisiae

  • 장원진;안진현;고광호;강현삼
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.295-295
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    • 1994
  • The human ${\beta}$$_2$-adrenergic receptor (h${\beta}$$_2$AR) contains seven clusters of hydrophobic amino acids suggestive of membrane-spanning domains and its gene is intronless. The genomic gene encoding h${\beta}$$_2$AR has been isolated by polymerase chain reaction. To express h${\beta}$$_2$AR in Saccharomyces cerevisiae, a modified h${\beta}$$_2$AR gene was fused to signal peptide sequence of Killer toxin gene from Kluyveromyces lactics. This fusion gene was expressed under the galactose-inducible GAL10 promoter. The ligand binding experiments showed that the functional h${\beta}$$_2$AR was expressed at a concentration three times as much as that found in Hamster lung.

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