Interactions of neomycin with monomolecular films of polyphosphoinositides and other lipids
dc.contributor.author | Lodhi, Shahid | en_US |
dc.contributor.author | Weiner, Norman D. | en_US |
dc.contributor.author | Schacht, Jochen | en_US |
dc.date.accessioned | 2006-04-07T17:31:57Z | |
dc.date.available | 2006-04-07T17:31:57Z | |
dc.date.issued | 1979-10-19 | en_US |
dc.identifier.citation | Lodhi, Shahid, Weiner, Norman D., Schacht, Jochen (1979/10/19)."Interactions of neomycin with monomolecular films of polyphosphoinositides and other lipids." Biochimica et Biophysica Acta (BBA) - Biomembranes 557(1): 1-8. <http://hdl.handle.net/2027.42/23471> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1T-47T317T-2W/2/1aff9627357f7dd156d0c16f2851a092 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23471 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=232987&dopt=citation | en_US |
dc.description.abstract | The interactions of calcium and the aminoglycosidic antibiotic, neomycin, with various lipids were investigated in monomolecular films. Lipids were spread over a subphase of 0.05 M N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid, pH 7.0, and NaCl to give an ionic strength of 0.2. Measurements of surface pressure ([pi]) were taken with a Wilhelmy balance. In the absence of Ca2+, 1 [mu]M-1 mM neomycin in the subphase decreased [pi] (i.e. condensed films) of all acidic lipids tested. In the presence of 1 mM Ca2+, neomycin did not change [pi] of films of phosphatidylserine, phosphatidylinositol and phosphatidic acid while it lowered [pi] of cardiolipin and cerebroside sulfate films. A unique pattern of interaction was observed with polyphosphoinositide monolayers. In the absence of Ca2+, 1 [mu]M neomycin decreased [pi] followed by an increase of [pi] at higher neomycin concentrations. Ca2+ (1 mM) condensed the film significantly more than did neomycin. However, as little as 1 [mu]M neomycin induced expansion of the calcium/lipid film which at 1 mM neomycin reached the same [pi] as in the absence of Ca2+. Such expansion was observed at all pressures of the film including the collapse pressure indicating a strong `complex' between the drug and polyphosphoinositide not antagonized by Ca2+. In the absence of possible hydrophobic interactions, both the condensation and the expansion of the film should be mediated by ionic forces. Combined in vivo and in vitro evidence is discussed to suggest the polyphosphoinositides as the physiological receptors for aminoglycosides in the mammalian cell membrane. | en_US |
dc.format.extent | 521420 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Interactions of neomycin with monomolecular films of polyphosphoinositides and other lipids | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | ollege of Pharmacy, Kresge Hearing Research Institute and Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | ollege of Pharmacy, Kresge Hearing Research Institute and Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | ollege of Pharmacy, Kresge Hearing Research Institute and Department of Biological Chemistry, The University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 232987 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23471/1/0000424.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2736(79)90084-1 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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