Physicochemical properties of hepatitis B peptide fragments at the air-water and lipid-water interfaces

M. A. Alsina; C. Mestres; F. Rabanal; M. A. Busquets; F. Reig

doi:10.1016/0040-6090(92)90393-P

Physicochemical properties of hepatitis B peptide fragments at the air-water and lipid-water interfaces

M. A. Alsina^*, C. Mestres, F. Rabanal, M. A. Busquets, F. Reig

^*Corresponding author for this work

Research output: Indexed journal article › Article › peer-review

Abstract

In the present paper the interaction of four lipopeptides derived from the Pre S (120-145) sequence of the hepatitis B virus (HBV) with different lipids is described. The parent peptide structure was MQWNSTALHQALQDPRVGLYLPAGG. The peptide derivatives contained a residue of Pam₃CSS, cholanoyl and stearoyl residues attached to their amino terminal end in order to modify the hydrophobicity of the peptide and to improve their potential antigenicity. The interactions have been studied using compression isotherms of monolayers and penetration kinetics. All the peptides showed surface activity and formed stable monolayers. The presence of these peptides under a monolayer of DPPC caused an expansion in the area occupied per molecule and modified the phase change of the DPPC.

Original language	English
Pages (from-to)	750-752
Number of pages	3
Journal	Thin Solid Films
Volume	210-211
Issue number	PART 2
DOIs	https://doi.org/10.1016/0040-6090(92)90393-P
Publication status	Published - 30 Apr 1992
Externally published	Yes

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title = "Physicochemical properties of hepatitis B peptide fragments at the air-water and lipid-water interfaces",

abstract = "In the present paper the interaction of four lipopeptides derived from the Pre S (120-145) sequence of the hepatitis B virus (HBV) with different lipids is described. The parent peptide structure was MQWNSTALHQALQDPRVGLYLPAGG. The peptide derivatives contained a residue of Pam3CSS, cholanoyl and stearoyl residues attached to their amino terminal end in order to modify the hydrophobicity of the peptide and to improve their potential antigenicity. The interactions have been studied using compression isotherms of monolayers and penetration kinetics. All the peptides showed surface activity and formed stable monolayers. The presence of these peptides under a monolayer of DPPC caused an expansion in the area occupied per molecule and modified the phase change of the DPPC.",

author = "Alsina, {M. A.} and C. Mestres and F. Rabanal and Busquets, {M. A.} and F. Reig",

year = "1992",

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doi = "10.1016/0040-6090(92)90393-P",

language = "English",

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T1 - Physicochemical properties of hepatitis B peptide fragments at the air-water and lipid-water interfaces

AU - Alsina, M. A.

AU - Mestres, C.

AU - Rabanal, F.

AU - Busquets, M. A.

AU - Reig, F.

PY - 1992/4/30

Y1 - 1992/4/30

N2 - In the present paper the interaction of four lipopeptides derived from the Pre S (120-145) sequence of the hepatitis B virus (HBV) with different lipids is described. The parent peptide structure was MQWNSTALHQALQDPRVGLYLPAGG. The peptide derivatives contained a residue of Pam3CSS, cholanoyl and stearoyl residues attached to their amino terminal end in order to modify the hydrophobicity of the peptide and to improve their potential antigenicity. The interactions have been studied using compression isotherms of monolayers and penetration kinetics. All the peptides showed surface activity and formed stable monolayers. The presence of these peptides under a monolayer of DPPC caused an expansion in the area occupied per molecule and modified the phase change of the DPPC.

AB - In the present paper the interaction of four lipopeptides derived from the Pre S (120-145) sequence of the hepatitis B virus (HBV) with different lipids is described. The parent peptide structure was MQWNSTALHQALQDPRVGLYLPAGG. The peptide derivatives contained a residue of Pam3CSS, cholanoyl and stearoyl residues attached to their amino terminal end in order to modify the hydrophobicity of the peptide and to improve their potential antigenicity. The interactions have been studied using compression isotherms of monolayers and penetration kinetics. All the peptides showed surface activity and formed stable monolayers. The presence of these peptides under a monolayer of DPPC caused an expansion in the area occupied per molecule and modified the phase change of the DPPC.

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U2 - 10.1016/0040-6090(92)90393-P

DO - 10.1016/0040-6090(92)90393-P

M3 - Article

AN - SCOPUS:44049115951

SN - 0040-6090

VL - 210-211

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EP - 752

JO - Thin Solid Films

JF - Thin Solid Films

IS - PART 2

ER -

Physicochemical properties of hepatitis B peptide fragments at the air-water and lipid-water interfaces

Abstract

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