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  • In this article, we describe the mutual structural effect of the interaction between the model membranes and polylysine and poly-L-arginine. Vibrational circular dichroism (VCD), a method exceptionally sensitive to the polypeptide structure that has not been established in such studies before, was the primary method of this study. A complementary technique, electronic circular dichroism, was applied to verify the newly obtained results and as a bridge to the previous studies. We used micelles composed of sodium dodecyl sulfate (SDS) as a monolayer membrane model and large unilamellar vesicles composed of phospholipids as a bilayer membrane model. We describe the conformational changes of the polypeptides caused by the interaction with the model membranes. Among others, the presence of the liposomes in the solution generated special conditions for the formation of the alpha-helical structure of poly-L-arginine; the presence of SDS induced the formation of the beta-structure of polylysine. From a methodological point of view, we emphasize the advantages of infrared spectroscopic techniques for the liposomic membrane studies as well as the preference of ultraviolet techniques for smaller micellar systems.
  • In this article, we describe the mutual structural effect of the interaction between the model membranes and polylysine and poly-L-arginine. Vibrational circular dichroism (VCD), a method exceptionally sensitive to the polypeptide structure that has not been established in such studies before, was the primary method of this study. A complementary technique, electronic circular dichroism, was applied to verify the newly obtained results and as a bridge to the previous studies. We used micelles composed of sodium dodecyl sulfate (SDS) as a monolayer membrane model and large unilamellar vesicles composed of phospholipids as a bilayer membrane model. We describe the conformational changes of the polypeptides caused by the interaction with the model membranes. Among others, the presence of the liposomes in the solution generated special conditions for the formation of the alpha-helical structure of poly-L-arginine; the presence of SDS induced the formation of the beta-structure of polylysine. From a methodological point of view, we emphasize the advantages of infrared spectroscopic techniques for the liposomic membrane studies as well as the preference of ultraviolet techniques for smaller micellar systems. (en)
Title
  • Vibrational circular dichroism study of polypeptide model-membrane systems
  • Vibrational circular dichroism study of polypeptide model-membrane systems (en)
skos:prefLabel
  • Vibrational circular dichroism study of polypeptide model-membrane systems
  • Vibrational circular dichroism study of polypeptide model-membrane systems (en)
skos:notation
  • RIV/60461373:22340/12:43893351!RIV13-MSM-22340___
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  • S
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  • 2
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  • 177401
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  • RIV/60461373:22340/12:43893351
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  • Polypeptide-lipid interaction; Polypeptide-surfactant interaction; Micelle; Liposome; Vibrational circular dichroism; Polypeptide-membrane structure (en)
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  • US - Spojené státy americké
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  • [8B3AF828E631]
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  • Analytical Biochemistry
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  • 427
http://linked.open...iv/tvurceVysledku
  • Urbanová, Marie
  • Novotná, Pavlína
http://linked.open...ain/vavai/riv/wos
  • 000306872200019
issn
  • 0003-2697
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.ab.2012.03.023
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  • 22340
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