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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Phenylalanine interaction with lipid monolayers at different pHs.

A C Cutró1, A Hollmann1, J Cejas1

  • 1Laboratorio de Biointerfases y Sistemas Biomiméticos, Laboratorios Centrales, CITSE-UNSE, Santiago del Estero, Argentina.

Colloids and Surfaces. B, Biointerfaces
|August 19, 2015
PubMed
Summary

Phenylalanine (Phe) alters the surface pressure of lipid monolayers. At pH 5, Phe intercalates into DPPC films, but forms a different structure at pH 7.3.

Keywords:
DPPCDipole potential-pHLipid monolayersPhenylalanineSurface pressure

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Area of Science:

  • Biophysics
  • Surface Chemistry
  • Lipid Monolayers

Background:

  • Lipid monolayers at the air-water interface are crucial models for biological membranes.
  • Understanding the interaction of amino acids with lipids is essential for physiological studies.

Purpose of the Study:

  • To investigate the influence of phenylalanine (Phe) on the surface pressure and dipole potential of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) monolayers.
  • To analyze the effect of pH on Phe-DPPC interactions and monolayer compressibility.

Main Methods:

  • Measurement of surface pressure and dipole potential changes at fixed area.
  • Analysis of (π-A) isotherms to study compressibility properties at different pHs (5.0 and 7.3).
  • Experiments conducted at constant temperature (20 °C) and varying initial surface pressures (26 and 40 mN/m).

Main Results:

  • Phenylalanine (Phe) significantly affects the surface pressure of DPPC monolayers.
  • Evidence suggests Phe intercalates into DPPC films at pH 5.0.
  • A distinct arrangement of Phe within the DPPC monolayer is observed at pH 7.3.

Conclusions:

  • The interaction of phenylalanine with DPPC monolayers is pH-dependent.
  • Phe exhibits different intercalation and structural arrangements in DPPC films based on subphase pH.
  • These findings provide insights into the behavior of amino acids at interfaces relevant to physiological conditions.