Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

P. Sospedra; M. Muñoz; M. García; M. A. Alsina; C. Mestres; I. Haro

doi:10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.CO;2-L

Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

P. Sospedra, M. Muñoz, M. García, M. A. Alsina, C. Mestres, I. Haro^*

^*Corresponding author for this work

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

8 Citations (Scopus)

Abstract

Shorter analogues of a continuous epitope of hepatitis A virus, VP3(110-121) peptide, failed to react with convalescent sera, indicating the importance of the entire peptide in the epitope structure. To better understand the influence of the structural properties of the 12-mer peptide epitope on its biological activity, the interaction of smaller peptide analogues with phospholipid biomembrane models was investigated by a combination of spectroscopic and biophysical techniques. In this article we describe our findings concerning the surface activity and the interaction of peptides with simple mono- and bilayer membranes composed of a zwitterionic phospholipid (dipalmitoyl phosphatidylcholine, DPPC), an anionic phospholipid (dipalmitoyl phosphatidylglicerol, DPPG), or a DPPC/DPPG mixture. The results indicate that the net negative charge of the peptide is in some way responsible of the specific interactions between VP3(110-121) and membrane phospholipids, and necessary to induce β-type conformations upon vesicle interaction.

Original language	English
Pages (from-to)	477-488
Number of pages	12
Journal	Biopolymers
Volume	54
Issue number	7
DOIs	https://doi.org/10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.CO;2-L
Publication status	Published - Dec 2000
Externally published	Yes

Keywords

Biomembrane models
CD
Fluorescence
Hepatitis A virus
Monolayers
Synthetic peptides

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.CO;2-L

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title = "Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models",

abstract = "Shorter analogues of a continuous epitope of hepatitis A virus, VP3(110-121) peptide, failed to react with convalescent sera, indicating the importance of the entire peptide in the epitope structure. To better understand the influence of the structural properties of the 12-mer peptide epitope on its biological activity, the interaction of smaller peptide analogues with phospholipid biomembrane models was investigated by a combination of spectroscopic and biophysical techniques. In this article we describe our findings concerning the surface activity and the interaction of peptides with simple mono- and bilayer membranes composed of a zwitterionic phospholipid (dipalmitoyl phosphatidylcholine, DPPC), an anionic phospholipid (dipalmitoyl phosphatidylglicerol, DPPG), or a DPPC/DPPG mixture. The results indicate that the net negative charge of the peptide is in some way responsible of the specific interactions between VP3(110-121) and membrane phospholipids, and necessary to induce β-type conformations upon vesicle interaction.",

keywords = "Biomembrane models, CD, Fluorescence, Hepatitis A virus, Monolayers, Synthetic peptides",

author = "P. Sospedra and M. Mu{\~n}oz and M. Garc{\'i}a and Alsina, {M. A.} and C. Mestres and I. Haro",

year = "2000",

month = dec,

doi = "10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.CO;2-L",

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volume = "54",

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T1 - Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

AU - Sospedra, P.

AU - Muñoz, M.

AU - García, M.

AU - Alsina, M. A.

AU - Mestres, C.

AU - Haro, I.

PY - 2000/12

Y1 - 2000/12

N2 - Shorter analogues of a continuous epitope of hepatitis A virus, VP3(110-121) peptide, failed to react with convalescent sera, indicating the importance of the entire peptide in the epitope structure. To better understand the influence of the structural properties of the 12-mer peptide epitope on its biological activity, the interaction of smaller peptide analogues with phospholipid biomembrane models was investigated by a combination of spectroscopic and biophysical techniques. In this article we describe our findings concerning the surface activity and the interaction of peptides with simple mono- and bilayer membranes composed of a zwitterionic phospholipid (dipalmitoyl phosphatidylcholine, DPPC), an anionic phospholipid (dipalmitoyl phosphatidylglicerol, DPPG), or a DPPC/DPPG mixture. The results indicate that the net negative charge of the peptide is in some way responsible of the specific interactions between VP3(110-121) and membrane phospholipids, and necessary to induce β-type conformations upon vesicle interaction.

AB - Shorter analogues of a continuous epitope of hepatitis A virus, VP3(110-121) peptide, failed to react with convalescent sera, indicating the importance of the entire peptide in the epitope structure. To better understand the influence of the structural properties of the 12-mer peptide epitope on its biological activity, the interaction of smaller peptide analogues with phospholipid biomembrane models was investigated by a combination of spectroscopic and biophysical techniques. In this article we describe our findings concerning the surface activity and the interaction of peptides with simple mono- and bilayer membranes composed of a zwitterionic phospholipid (dipalmitoyl phosphatidylcholine, DPPC), an anionic phospholipid (dipalmitoyl phosphatidylglicerol, DPPG), or a DPPC/DPPG mixture. The results indicate that the net negative charge of the peptide is in some way responsible of the specific interactions between VP3(110-121) and membrane phospholipids, and necessary to induce β-type conformations upon vesicle interaction.

KW - Biomembrane models

KW - CD

KW - Fluorescence

KW - Hepatitis A virus

KW - Monolayers

KW - Synthetic peptides

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DO - 10.1002/1097-0282(200012)54:7<477::AID-BIP10>3.0.CO;2-L

M3 - Article

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AN - SCOPUS:0034578642

SN - 0006-3525

VL - 54

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EP - 488

JO - Biopolymers

JF - Biopolymers

IS - 7

ER -

Effect of chain length of HAV-VP3 synthetic peptides on its interaction with biomembrane models

Abstract

Keywords

UN SDGs

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