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      Hydration Shells of DPPC Liposomes from the Point of View of Terahertz Time-Domain Spectroscopy.

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          Abstract

          Analysis of structural and dynamic properties of water in suspensions of liposomes composed from 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) in three phase states (gel, rippled gel, liquid crystalline phase) by means of terahertz time-domain spectroscopy in 0.3-3.3 THz range was conducted in the current work. Fraction of free water molecules in DPPC liposome suspension was shown to decrease with temperature (compared to the analogous aqueous solution without liposomes), and intermolecular water binding was enhanced. The most crucial changes occur during gel-rippled gel phase transition (pretransition): at temperatures below pretransition point, liposomes alleviate water binding degree, while at temperatures above the transition point, they enhance water binding. This study has demonstrated the high information content of the terahertz time-domain spectroscopy method for exploring the hydration properties of phospholipids in water.

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          Author and article information

          Journal
          Appl Spectrosc
          Applied spectroscopy
          SAGE Publications
          1943-3530
          0003-7028
          Feb 2021
          : 75
          : 2
          Affiliations
          [1 ] Institute of Cell Biophysics of the Russian Academy of Sciences-Federal Research Center, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, Russia.
          [2 ] Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia.
          [3 ] Mari State University, Yoshkar-Ola, Russia.
          Article
          10.1177/0003702820949285
          32705897
          e981f09f-f68d-4df2-bdf9-c14d94e6629a
          History

          pretransition,water structure,large unilamellar vesicles,hydration shells,gel-rippled gel phase transition,THz-TDS,LUV

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