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X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers.

X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers. Research Abstract Details 

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  • X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers. Abstract Text:

    giyoong taeGiyoong Tae,hosung yangHosung Yang,kwanwoo shinKwanwoo Shin,sushil k satijaSushil K Satija,naoya torikaiNaoya Torikai,

    The penetration of a transcription-activating factor (TAT)-derived, cell-penetration peptide onto 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) or 1,2-dipalmitoyl-sn-glycero-3-[phospho-L-serine] (DPPS) monolayer on phosphate-buffered saline subphase was characterized. The surface area at the target pressure increased noticeably by the peptide penetration from the subphase to the phospholipid monolayer, which might suggest a direct penetration of the peptide across the pure phospholipid bilayer membrane. Interestingly, the more significant area increase at 35 mN/m was monitored from DPPC monolayer, contrary to the simple charge interaction: the net neutral DPPC, the net-negative DPPS, and the positive TAT-derived peptides (TDP). X-ray reflectivity measurements as well as the molecular area from pi (surface pressure)-A (area) isotherms suggest that the packing density of DPPS at the target pressure is too high to allow the effective penetration of the peptide into the monolayer and the positively charged peptides can be entrapped at the negative electrostatic well of DPPS headgroup layer, leading to the simple adsorption on the DPPS monolayer instead of penetration into it. Thus, more penetration with less adsorption of the peptide is induced by DPPC monolayer than DPPS monolayer. Copyright (c) 2007 European Peptide Society and John Wiley & Sons, Ltd.

    X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers. Publishing Authors By Initials

    g taeG Tae,h yangH Yang,k shinK Shin,sk satijaSK Satija,n torikaiN Torikai,

    For similar abstracts research abstracts see: abstracts research

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    X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of peptide science : an official publicati

    VOLUME: 14

    Page Numbers: 461-8

    Journal Abbreviation: J. Pept. Sci.

    ISSN: 1075-2617

    DAY: 25

    MONTH: Apr

    YEAR: 2008

    X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers. Information

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    LANGUAGE: eng

    NlmUniqueID: 9506309

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    Grant and Affiliation Information for X-ray reflectivity study of a transcription-activating factor-derived peptide penetration into the model phospholipid monolayers.

    AFFILIATION: Department of Materials Science and Engineering, GIST, Gwangju, Korea.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: J Pept Sci

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