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107. Polyene antibiotic that inhibits membrane transport proteins

Author

Te Welscher, Y.M., van Leeuwen, M.R., de Kruijff, B., Dijksterhuis, J., Breukink, E., Te Welscher, Y.M., van Leeuwen, M.R., de Kruijff, B., Dijksterhuis, J., and Breukink, E.

Abstract

The limited therapeutic arsenal and the increase in reports of fungal resistance to multiple antifungal agents have made fungal infections a major therapeutic challenge. The polyene antibiotics are the only group of antifungal antibiotics that directly target the plasma membrane via a specific interaction with the main fungal sterol, ergosterol, often resulting in membrane permeabilization. In contrast to other polyene antibiotics that form pores in the membrane, the mode of action of natamycin has remained obscure but is not related to membrane permeabilization. Here, we demonstrate that natamycin inhibits growth of yeasts and fungi via the immediate inhibition of amino acid and glucose transport across the plasma membrane. This is attributable to ergosterol-specific and reversible inhibition of membrane transport proteins. It is proposed that ergosterol-dependent inhibition of membrane proteins is a general mode of action of all the polyene antibiotics, of which some have been shown additionally to permeabilize the plasma membrane. Our results imply that sterol-protein interactions are fundamentally important for protein function even for those proteins that are not known to reside in sterol-rich domains., The limited therapeutic arsenal and the increase in reports of fungal resistance to multiple antifungal agents have made fungal infections a major therapeutic challenge. The polyene antibiotics are the only group of antifungal antibiotics that directly target the plasma membrane via a specific interaction with the main fungal sterol, ergosterol, often resulting in membrane permeabilization. In contrast to other polyene antibiotics that form pores in the membrane, the mode of action of natamycin has remained obscure but is not related to membrane permeabilization. Here, we demonstrate that natamycin inhibits growth of yeasts and fungi via the immediate inhibition of amino acid and glucose transport across the plasma membrane. This is attributable to ergosterol-specific and reversible inhibition of membrane transport proteins. It is proposed that ergosterol-dependent inhibition of membrane proteins is a general mode of action of all the polyene antibiotics, of which some have been shown additionally to permeabilize the plasma membrane. Our results imply that sterol-protein interactions are fundamentally important for protein function even for those proteins that are not known to reside in sterol-rich domains.

Published
2012

108. Structure, dynamics, and insertion of a chloroplast targeting peptide in mixed micelles

Author

Hans Wienk, Michael Czisch, de Kruijff B, and Rainer Wechselberger

Subjects
chemistry.chemical_classification, Circular dichroism, Chloroplasts, Magnetic Resonance Spectroscopy, Chemistry, Protein Conformation, Membrane lipids, Circular Dichroism, digestive, oral, and skin physiology, Molecular Sequence Data, Peptide, Biochemistry, Micelle, Chloroplast membrane, Crystallography, Magnoliopsida, Heteronuclear molecule, Transit Peptide, Biophysics, Ferredoxins, Amino Acid Sequence, Structural motif, Peptides, Micelles
Abstract

Nuclear-encoded, chloroplast-destined proteins are synthesized with transit sequences that contain all information to get them inside the organelle. Different proteins are imported via a general protein import machinery, but their transit sequences do not share amino acid homology. It has been suggested that interactions between transit sequence and chloroplast envelope membrane lipids give rise to recognizable, structural motifs. In this study a detailed investigation of the structural, dynamical, and topological features of an isolated transit peptide associated with mixed micelles is described. The structure of the preferredoxin transit peptide in these micelles was studied by circular dichroism (CD) and multidimensional NMR techniques. CD experiments indicated that the peptide, which is unstructured in aqueous solution, obtained helical structure in the presence of the micelles. By NMR it is shown that the micelles introduced ill-defined helical structures in the transit peptide. Heteronuclear relaxation experiments showed that the whole peptide backbone is very flexible. The least dynamic segments are two N- and C-terminal helical regions flanking an unstructured proline-rich amino acid stretch. Finally, the insertion of the peptide backbone in the hydrophobic interior of the micelle was investigated by use of hydrophobic spin-labels. The combined data result in a model of the transit peptide structure, backbone dynamics, and insertion upon its interaction with mixed micelles.

Published
2000

109. Visualization of highly ordered striated domains induced by transmembrane peptides in supported phosphatidylcholine bilayers

Author

van Der Eerden Jp, Rudy A. Demel, Margot M. E. Snel, de Kruijff B, J.A. Killian, Hilde A. Rinia, and Kik Ra

Subjects
chemistry.chemical_classification, Models, Molecular, Vesicle fusion, 1,2-Dipalmitoylphosphatidylcholine, Bilayer, Vesicle, Lipid Bilayers, Phospholipid, Membrane Proteins, Peptide, Microscopy, Atomic Force, Biochemistry, Protein Structure, Secondary, Amino acid, Protein Structure, Tertiary, chemistry.chemical_compound, Crystallography, Protein structure, chemistry, Phosphatidylcholine, Phosphatidylcholines, Thermodynamics, Peptides
Abstract

We used atomic force microscopy (AFM) to study the lateral organization of transmembrane TmAW(2)(LA)(n)W(2)Etn peptides (WALP peptides) incorporated in phospholipid bilayers. These well-studied model peptides consist of a hydrophobic alanine-leucine stretch of variable length, flanked on each side by two tryptophans. They were incorporated in saturated phosphatidylcholine (PC) vesicles, which were deposited on a solid substrate via the vesicle fusion method, yielding hydrated gel-state supported bilayers. At low concentrations (1 mol %) WALP peptides induced primarily line-type depressions in the bilayer. In addition, striated lateral domains were observed, which increased in amount and size (from 25 nm up to 10 microm) upon increasing peptide concentration. At high peptide concentration (10 mol %), the bilayer consisted mainly of striated domains. The striated domains consist of line-type depressions and elevations with a repeat distance of 8 nm, which form an extremely ordered, predominantly hexagonal pattern. Overall, this pattern was independent of the length of the peptides (19-27 amino acids) and the length of the lipid acyl chains (16-18 carbon atoms). The striated domains could be pushed down reversibly by the AFM tip and are thermodynamically stable. This is the first direct visualization of alpha-helical transmembrane peptide-lipid domains in a bilayer. We propose that these striated domains consist of arrays of WALP peptides and fluidlike PC molecules, which appear as low lines. The presence of the peptides perturbs the bilayer organization, resulting in a decrease in the tilt of the lipids between the peptide arrays. These lipids therefore appear as high lines.

Published
2000

110. Engineering a disulfide bond and free thiols in the lantibiotic nisin Z

Author

van Kraaij, C, Breukink, E, Rollema, HS, Bongers, RS, Kosters, HA, de Kruijff, B, Kuipers, OP, Rollema, Harry S., Bongers, Roger S., Groningen Biomolecular Sciences and Biotechnology, and Molecular Genetics

Subjects
Lactococcus lactis, IDENTIFICATION, CYSTEINE-SCANNING MUTAGENESIS, RESIDUES, nisin, protein engineering, BIOSYNTHESIS, C-TERMINAL PART, MEMBRANE, LACTOCOCCUS-LACTIS, cysteine, CHEMICAL MODIFICATION, mutagenesis
Abstract

The antimicrobial peptide nisin contains the uncommon amino acid residues lanthionine and methyl-lanthionine, which are post-translationally formed from Ser, Thr and Cys residues. To investigate the importance of these uncommon residues for nisin activity, a mutant was designed in which Thr13 was replaced by a Cys residue, which prevents the formation of the thioether bond of ring C. Instead, Cys13 couples with Cys19 via an intramolecular disulfide bridge, a bond that is very unusual in lantibiotics. NMR analysis of this mutant showed a structure very similar to that of wild-type nisin, except for the configuration of ring C. The modification was accompanied by a dramatic reduction in antimicrobial activity to less than 1% of wild-type activity, indicating that the lanthionine of ring C is very important for this activity. The nisin Z mutants S5C and M17C were also isolated and characterized; they are the first lantibiotics known that contain an additional Cys residue that is not involved in bridge formation but is present as a free thiol. Secretion of these peptides by the lactococcal producer cells, as well as their antimicrobial activity, was found to be strongly dependent on a reducing environment. Their ability to permeabilize lipid vesicles was not thiol-dependent. Labeling of M17C nisin Z with iodoacetamide abolished the thiol-dependence of the peptide. These results show that the presence of a reactive Cys residue in nisin has a strong effect on the antimicrobial properties of the peptide, which is probably the result of interaction of these residues with thiol groups on the outside of bacterial cells.

Published
2000

111. Natamycin inhibits vacuole fusion at the priming phase via a specific interaction with ergosterol

Author

Biochemistry of membranes, Molecular Microbiology, Sub Biochemistry of Membranes begr1-6-12, Sub Molecular Microbiology, Sub Algemeen Scheikunde, te Welscher, Y.M., Jones, L., van Leeuwen, M.R., Dijksterhuis, J., de Kruijff, B., Eitzen, G., Breukink, E.J., Biochemistry of membranes, Molecular Microbiology, Sub Biochemistry of Membranes begr1-6-12, Sub Molecular Microbiology, Sub Algemeen Scheikunde, te Welscher, Y.M., Jones, L., van Leeuwen, M.R., Dijksterhuis, J., de Kruijff, B., Eitzen, G., and Breukink, E.J.

Published
2010

112. Self-reproduction of fatty acid vesicles: a combined experimental and simulation study

Author

Biochemistry of membranes, Sub Biochemistry of Membranes begr1-6-12, Dep Scheikunde, Sub Algemeen Scheikunde, Markvoort, A.J., Pfleger, N., Staffhorst, R.W.H.M., Hilbers, P.A.J., van Santen, R.A., Killian, J.A., de Kruijff, B., Biochemistry of membranes, Sub Biochemistry of Membranes begr1-6-12, Dep Scheikunde, Sub Algemeen Scheikunde, Markvoort, A.J., Pfleger, N., Staffhorst, R.W.H.M., Hilbers, P.A.J., van Santen, R.A., Killian, J.A., and de Kruijff, B.

Published
2010

114. Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface

Author

Biomolecular Mass Spectrometry and Proteomics, Massaspectrometrie, Membrane Enzymology, SYNTHESE, Dep Farmaceutische wetenschappen, Sub Algemeen Scheikunde, Sub Medicinal Chemistry begr. 01-01-2014, Sub Membrane Enzymology begr. 01-06-12, Gubbens, J., Ruijter, E., Fays, L.E.V., Damen, J.M.A., de Kruijff, B., Slijper, M., Rijkers, D.T.S., Liskamp, R.M.J., de Kroon, A.I.P.M., Biomolecular Mass Spectrometry and Proteomics, Massaspectrometrie, Membrane Enzymology, SYNTHESE, Dep Farmaceutische wetenschappen, Sub Algemeen Scheikunde, Sub Medicinal Chemistry begr. 01-01-2014, Sub Membrane Enzymology begr. 01-06-12, Gubbens, J., Ruijter, E., Fays, L.E.V., Damen, J.M.A., de Kruijff, B., Slijper, M., Rijkers, D.T.S., Liskamp, R.M.J., and de Kroon, A.I.P.M.

Published
2009

115. Cardiolipin molecular species with shorter acyl chains accumulate in Saccharomyces cerevisiae mutants lacking the acyl coenzyme A-binding protein Acb1p: New insights into acyl chain remodeling of cardiolipin

Author

Biochemistry of membranes, Biology of Reproductive Cells, Membrane Enzymology, Strategic Infection Biology, Dep Biochemie en Celbiologie, Sub Biochemistry of Membranes begr1-6-12, Sub Algemeen Scheikunde, Sub Membrane Enzymology begr. 01-06-12, Rijken, P.J., Houtkooper, R.H., Akbari, H., Brouwers, J.F.H.M., Koorengevel, M.C., de Kruijff, B., Frentzen, M., Vaz, F.M., de Kroon, A.I.P.M., Biochemistry of membranes, Biology of Reproductive Cells, Membrane Enzymology, Strategic Infection Biology, Dep Biochemie en Celbiologie, Sub Biochemistry of Membranes begr1-6-12, Sub Algemeen Scheikunde, Sub Membrane Enzymology begr. 01-06-12, Rijken, P.J., Houtkooper, R.H., Akbari, H., Brouwers, J.F.H.M., Koorengevel, M.C., de Kruijff, B., Frentzen, M., Vaz, F.M., and de Kroon, A.I.P.M.

Published
2009

116. Potential scorpionate antibiotics: targeted hydrolysis of lipid II containing model membranes by vancomycin-TACzyme conjugates and modulation of their antibacterial activity by Zn-ions

Author

Biochemie van Membranen, Biochemistry of membranes, Chemical Biology & Organic Chemistry, Medicinal Chemistry, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Sub Algemeen Scheikunde, Sub Medicinal Chemistry begr. 01-01-2014, Albada, H.B., Arnusch, C.J., Branderhorst, H.M., Verel, A.M., Janssen, W.T.M., Breukink, E.J., de Kruijff, B., Pieters, R.J., Liskamp, R.M.J., Biochemie van Membranen, Biochemistry of membranes, Chemical Biology & Organic Chemistry, Medicinal Chemistry, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Sub Algemeen Scheikunde, Sub Medicinal Chemistry begr. 01-01-2014, Albada, H.B., Arnusch, C.J., Branderhorst, H.M., Verel, A.M., Janssen, W.T.M., Breukink, E.J., de Kruijff, B., Pieters, R.J., and Liskamp, R.M.J.

Published
2009

117. High cytotoxicity of cisplatin nanocapsules in ovarian carcinoma cells depends on uptake by caveolae-mediated endocytosis

Author

Biochemie van Membranen, Membrane Enzymology, Dep Scheikunde, Dep Biologie, Hamelers, I.H.L., Staffhorst, R.W.H.M., Voortman, J., de Kruijff, B., Reedijk, J., van Bergen en Henegouwen, P.M.P., de Kroon, A.I.P.M., Biochemie van Membranen, Membrane Enzymology, Dep Scheikunde, Dep Biologie, Hamelers, I.H.L., Staffhorst, R.W.H.M., Voortman, J., de Kruijff, B., Reedijk, J., van Bergen en Henegouwen, P.M.P., and de Kroon, A.I.P.M.

Published
2009

118. Lipid II:a central component in bacterial cell wall synthesis and a target for antibiotics

Author

de Kruijff, B., van Dam, V., Breukink, E.J., de Kruijff, B., van Dam, V., and Breukink, E.J.

Abstract

The bacterial cell wall is mainly composed of peptidoglycan, which is a three-dimensional network of long aminosugar strands located on the exterior of the cytoplasmic membrane. These strands consist of alternating MurNAc and GlcNAc units and are interlinked to each other via peptide moieties that are attached to the MurNAc residues. Peptidoglycan subunits are assembled on the cytoplasmic side of the bacterial membrane on a polyisoprenoid anchor and one of the key components in the synthesis of peptidoglycan is Lipid II. Being essential for bacterial cell survival, it forms an attractive target for antibacterial compounds such as vancomycin and several lantibiotics. Lipid II consists of one GlcNAc-MurNAc-pentapeptide subunit linked to a polyiosoprenoid anchor 11 subunits long via a pyrophosphate linker. This review focuses on this special molecule and addresses three questions. First, why are special lipid carriers as polyprenols used in the assembly of peptidoglycan? Secondly, how is Lipid II translocated across the bacterial cytoplasmic membrane? And finally, how is Lipid II used as a receptor for lantibiotics to kill bacteria?

Published
2008

120. Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Molecular Cell Biology, Dep Scheikunde, Sub Inorganic Chemistry and Catalysis, Dep Biologie, Engel, M.F.M., Khemtemourian, L.P., Kleijer, C.C., Meeldijk, J.D., Jacobs, J., Verkleij, A.J., de Kruijff, B., Killian, J.A., Hoppener, J.W.M., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Molecular Cell Biology, Dep Scheikunde, Sub Inorganic Chemistry and Catalysis, Dep Biologie, Engel, M.F.M., Khemtemourian, L.P., Kleijer, C.C., Meeldijk, J.D., Jacobs, J., Verkleij, A.J., de Kruijff, B., Killian, J.A., and Hoppener, J.W.M.

Published
2008

121. Natamycin blocks fungal growth by binding specifically to ergosterol without permeabilizing the membrane

Author

Biochemie van Membranen, Biochemistry of membranes, Membraan enzymologie, Dep Scheikunde, te Welscher, Y.M., ten Napel, H.H., Masià Balagué, M., Souza, C.M., Riezman, H., de Kruijff, B., Breukink, E.J., Biochemie van Membranen, Biochemistry of membranes, Membraan enzymologie, Dep Scheikunde, te Welscher, Y.M., ten Napel, H.H., Masià Balagué, M., Souza, C.M., Riezman, H., de Kruijff, B., and Breukink, E.J.

Published
2008

122. Protein complexes in bacterial and yeast mitochondrial membranes differ in their sensitivity towards dissociation by SDS

Author

Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Chemical Biology & Organic Chemistry, Massaspectrometrie, Membraan enzymologie, Dep Farmaceutische wetenschappen, Dep Scheikunde, Gubbens, J., Slijper, M., de Kruijff, B., de Kroon, A.I.P.M., Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Chemical Biology & Organic Chemistry, Massaspectrometrie, Membraan enzymologie, Dep Farmaceutische wetenschappen, Dep Scheikunde, Gubbens, J., Slijper, M., de Kruijff, B., and de Kroon, A.I.P.M.

Published
2008

123. Protein self-assembly and lipid binding in the folding of the potassium channel KcsA

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Barrera, F.N., Renard, M.L., Poveda, J.A., de Kruijff, B., Killian, J.A., González-Ros, J.M., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Barrera, F.N., Renard, M.L., Poveda, J.A., de Kruijff, B., Killian, J.A., and González-Ros, J.M.

Published
2008

124. Increased D-alanylation of lipoteichoic acid and a thickened septum are main determinants in the nisin resistance mechanism of Lactococcus lactis

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Kramer, N.E., Hasper, H.E., van den Bogaard, P.T.C., Morath, S., de Kruijff, B., Hartung, T., Smid, E.J., Breukink, E.J., Kok, J., Kuipers, O.P., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Kramer, N.E., Hasper, H.E., van den Bogaard, P.T.C., Morath, S., de Kruijff, B., Hartung, T., Smid, E.J., Breukink, E.J., Kok, J., and Kuipers, O.P.

Published
2008

125. The vancomycin-nisin(1-12) hybrid restores activity against vancomycin resistant enterococci

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Medicinal Chemistry, NMR-spectroscopie, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Arnusch, C.J., Bonvin, A.M.J.J., Verel, A.M., Jansen, W.T.M., Liskamp, R.M.J., de Kruijff, B., Pieters, R.J., Breukink, E.J., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Medicinal Chemistry, NMR-spectroscopie, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Arnusch, C.J., Bonvin, A.M.J.J., Verel, A.M., Jansen, W.T.M., Liskamp, R.M.J., de Kruijff, B., Pieters, R.J., and Breukink, E.J.

Published
2008

126. Membrane organization and ionization behavior of the minor but crucial lipid ceramide-1-phosphate

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Kooijman, E.E., Slot, J., Montes, L.-R., Alonso, A., Gericke, A., de Kruijff, B., Kumar, S., Goñi, F.M., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Kooijman, E.E., Slot, J., Montes, L.-R., Alonso, A., Gericke, A., de Kruijff, B., Kumar, S., and Goñi, F.M.

Published
2008

127. Transmembrane transport of peptidoglycan precursors across model and bacterial membranes

Author

Biochemie van Membranen, Membraan enzymologie, Dep Scheikunde, Sub Membrane Enzymology begr. 01-06-12, Sub Algemeen Scheikunde, van Dam, V., Sijbrandi, R., Kol, M.A., Swiezewska, E., de Kruijff, B., Breukink, E.J., Biochemie van Membranen, Membraan enzymologie, Dep Scheikunde, Sub Membrane Enzymology begr. 01-06-12, Sub Algemeen Scheikunde, van Dam, V., Sijbrandi, R., Kol, M.A., Swiezewska, E., de Kruijff, B., and Breukink, E.J.

Published
2007

130. 2,2,2-Trifluoroethanol changes the transition kinetics and subunit interactions in the small bacterial mechanosensitive channel MscS

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Akitake, B., Spelbrink, R.E.J., Anishkin, A., Killian, J.A., de Kruijff, B., Sukharev, S., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Dep Scheikunde, Akitake, B., Spelbrink, R.E.J., Anishkin, A., Killian, J.A., de Kruijff, B., and Sukharev, S.

Published
2007

131. Enhanced membrane pore information by multimeric/oligomeric antimicrobial peptides

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, Medicinal Chemistry, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Arnusch, C.J., Branderhorst, H.M., de Kruijff, B., Liskamp, R.M.J., Breukink, E.J., Pieters, R.J., Biochemie van Membranen, Chemical Biology & Organic Chemistry, Medicinal Chemistry, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Arnusch, C.J., Branderhorst, H.M., de Kruijff, B., Liskamp, R.M.J., Breukink, E.J., and Pieters, R.J.

Published
2007

132. An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins

Author

Biochemie van Membranen, Chemical Biology & Organic Chemistry, SYNTHESE, Dep Scheikunde, Dep Farmaceutische wetenschappen, Dep Biologie, Kooijman, E.E., Tieleman, D.P., Testerink, C., Munnik, T., Rijkers, D.T.S., Burger, K.N.J., de Kruijff, B., Biochemie van Membranen, Chemical Biology & Organic Chemistry, SYNTHESE, Dep Scheikunde, Dep Farmaceutische wetenschappen, Dep Biologie, Kooijman, E.E., Tieleman, D.P., Testerink, C., Munnik, T., Rijkers, D.T.S., Burger, K.N.J., and de Kruijff, B.

Published
2007

133. Probing the membrane interface-interacting proteome using photactivatable lipid cross-linkers

Author

Advanced drug delivery systems/drug targeting, Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Chemical Biology & Organic Chemistry, Massaspectrometrie, Dep Scheikunde, Dep Farmaceutische wetenschappen, Gubbens, J, Vader, P., Damen, J.M.A., O'Flaherty, M.C., Slijper, M., de Kruijff, B., de Kroon, A.I.P.M., Advanced drug delivery systems/drug targeting, Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Chemical Biology & Organic Chemistry, Massaspectrometrie, Dep Scheikunde, Dep Farmaceutische wetenschappen, Gubbens, J, Vader, P., Damen, J.M.A., O'Flaherty, M.C., Slijper, M., de Kruijff, B., and de Kroon, A.I.P.M.

Published
2007

136. Nanocapsules: a new vehicle for intracellular delivery of drugs

Author

Biochemical Physiology, Biochemie van Membranen, Dep Scheikunde, Dep Biologie, de Kroon, A.I.P.M., Stafhorst, R.W.H.M., de Kruijff, B., Burger, K.N.J., Harris, R., Biochemical Physiology, Biochemie van Membranen, Dep Scheikunde, Dep Biologie, de Kroon, A.I.P.M., Stafhorst, R.W.H.M., de Kruijff, B., Burger, K.N.J., and Harris, R.

Published
2006

137. Islet amyloid polypeptide inserts into phospholipid monolayers as monomer

Author

Biochemie van Membranen, Biokatalyse, Medicinal Chemistry, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Engel, M.F.M., Yigittop, H., Elgersma, R.C., Rijkers, D.T.S., Liskamp, R.M.J., de Kruijff, B., Hoppener, J.W.M., Killian, J.A., Biochemie van Membranen, Biokatalyse, Medicinal Chemistry, SYNTHESE, Dep Farmaceutische wetenschappen, Dep Scheikunde, Engel, M.F.M., Yigittop, H., Elgersma, R.C., Rijkers, D.T.S., Liskamp, R.M.J., de Kruijff, B., Hoppener, J.W.M., and Killian, J.A.

Published
2006

138. Lipid II as a target for antibiotics

Author

Biochemie van Membranen, Dep Scheikunde, Breukink, E.J., de Kruijff, B., Biochemie van Membranen, Dep Scheikunde, Breukink, E.J., and de Kruijff, B.

Published
2006

140. Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: evidence for regulation of intrinsic membrane curvature in a eukaryote

Author

Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Dep Scheikunde, Boumann, H.A., Gubbens, J, Koorengevel, M.C., Oh, C-S., Martin, C.E., Heck, A.J.R., Patton-Vogt, J., Henry, S.A., de Kruijff, B., de Kroon, A.I.P.M., Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Dep Scheikunde, Boumann, H.A., Gubbens, J, Koorengevel, M.C., Oh, C-S., Martin, C.E., Heck, A.J.R., Patton-Vogt, J., Henry, S.A., de Kruijff, B., and de Kroon, A.I.P.M.

Published
2006

143. Detection and identification of stable oligomeric protein complexes in Escherichia coli inner membranes.

Author

Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Aandachtsgebieden, Dep Scheikunde, Dep Farmaceutische wetenschappen, Spelbrink, R.E.J., Kolkman, A., Slijper, M., Killian, J.A., de Kruijff, B., Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Aandachtsgebieden, Dep Scheikunde, Dep Farmaceutische wetenschappen, Spelbrink, R.E.J., Kolkman, A., Slijper, M., Killian, J.A., and de Kruijff, B.

Published
2005

144. Spontaneous curvature of phosphatidic acid and lysophosphatidic acid.

Author

Biochemie van Membranen, Aandachtsgebieden, Dep Scheikunde, Dep Biologie, Kooijman, E.E., Chupin, V.V., Fuller, N.L., Kozlov, M.M., de Kruijff, B., Burger, K.N.J., Rand, P.R., Biochemie van Membranen, Aandachtsgebieden, Dep Scheikunde, Dep Biologie, Kooijman, E.E., Chupin, V.V., Fuller, N.L., Kozlov, M.M., de Kruijff, B., Burger, K.N.J., and Rand, P.R.

Published
2005

145. Molecular organization in striated domains induced by transmembrane alpha-helical peptides in dipalmitoyl phosphatidylcholine bilayers

Author

Biochemie van Membranen, Grensvlakken, Kristal- en structuurchemie, SYNTHESE, Crystal and Structural Chemistry 1, Dep Scheikunde, Dep Farmaceutische wetenschappen, Sparr, E.M., Ganchev, D.N., Snel, M.M.E., Ridder, A.N.J.A., Kroon-Batenburg, L.M.J., Chupin, V.V., Rijkers, D.T.S., Killian, J.A., de Kruijff, B., Biochemie van Membranen, Grensvlakken, Kristal- en structuurchemie, SYNTHESE, Crystal and Structural Chemistry 1, Dep Scheikunde, Dep Farmaceutische wetenschappen, Sparr, E.M., Ganchev, D.N., Snel, M.M.E., Ridder, A.N.J.A., Kroon-Batenburg, L.M.J., Chupin, V.V., Rijkers, D.T.S., Killian, J.A., and de Kruijff, B.

Published
2005

146. Cisplatin nanocapsules.

Author

Biochemie van Membranen, Aandachtsgebieden, Dep Scheikunde, Dep Biologie, de Kroon, A.I.P.M., Staffhorst, R.W.H.M., de Kruijff, B., Burger, K.N.J., Biochemie van Membranen, Aandachtsgebieden, Dep Scheikunde, Dep Biologie, de Kroon, A.I.P.M., Staffhorst, R.W.H.M., de Kruijff, B., and Burger, K.N.J.

Published
2005

147. What makes the bioactive lipids phosphatidic acid and lysophosphatidic acid so special?

Author

Biochemie van Membranen, Aandachtsgebieden, Dep Scheikunde, Dep Biologie, Kooijman, E.E., Carter, K.M., van Laar, E.G., Chupin, V., Burger, K.N.J., de Kruijff, B., Biochemie van Membranen, Aandachtsgebieden, Dep Scheikunde, Dep Biologie, Kooijman, E.E., Carter, K.M., van Laar, E.G., Chupin, V., Burger, K.N.J., and de Kruijff, B.

Published
2005

148. A synergistic effect between cholesterol and tryptophan-flanked transmembrane helices modulates membrane curvature.

Author

Biochemie van Membranen, Heterogene katalyse en oppervlakteonderzoek, SYNTHESE, Inorganic Chemistry and Catalysis 1, Dep Scheikunde, Sub Inorganic Chemistry and Catalysis, Dep Biologie, Dep Farmaceutische wetenschappen, van Duyl, B.Y., Meeldijk, J.D., Verkleij, A.J., Rijkers, D.T.S., Chupin, V.V., de Kruijff, B., Killian, J.A., Biochemie van Membranen, Heterogene katalyse en oppervlakteonderzoek, SYNTHESE, Inorganic Chemistry and Catalysis 1, Dep Scheikunde, Sub Inorganic Chemistry and Catalysis, Dep Biologie, Dep Farmaceutische wetenschappen, van Duyl, B.Y., Meeldijk, J.D., Verkleij, A.J., Rijkers, D.T.S., Chupin, V.V., de Kruijff, B., and Killian, J.A.

Published
2005

149. The selective utilization of substrates in vivo by the phosphatidylethanolamine and phosphatidylcholine biosynthetic enzymes Ept1p and Cpt1p in yeast

Author

Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Aandachtsgebieden, Dep Scheikunde, Boumann, H.A., de Kruijff, B.|info:eu-repo/dai/nl/140952551, Heck, A.J.R.|info:eu-repo/dai/nl/105189332, de Kroon, A.I.P.M.|info:eu-repo/dai/nl/084765283, Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Aandachtsgebieden, Dep Scheikunde, Boumann, H.A., de Kruijff, B.|info:eu-repo/dai/nl/140952551, Heck, A.J.R.|info:eu-repo/dai/nl/105189332, and de Kroon, A.I.P.M.|info:eu-repo/dai/nl/084765283

Published
2004

150. Uptake and remodeling of exogenous phosphatidylethanolamine in E. coli

Author

Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Membraan enzymologie, Molecular Microbiology, Biomolecular Mass Spectrometry 1, Dep Scheikunde, Dep Biologie, Kol, M.A., Kuster, D.W.D., Boumann, H.A., de Cock, J.J.P.A., Heck, A.J.R., de Kruijff, B., de Kroon, A.I.P.M., Biochemie van Membranen, Biomoleculaire Massaspectrometrie, Massaspectrometrie, Membraan enzymologie, Molecular Microbiology, Biomolecular Mass Spectrometry 1, Dep Scheikunde, Dep Biologie, Kol, M.A., Kuster, D.W.D., Boumann, H.A., de Cock, J.J.P.A., Heck, A.J.R., de Kruijff, B., and de Kroon, A.I.P.M.

Published
2004

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