P59, a 20-mer peptide modeled on the membrane-proximal external region (MPER) of the feline immunodeficiency virus (FIV) gp36 ectodomain, has potent antiviral activity. The lipoylated analogue, lipo-P59, displays a similar activity, which is preferentially retained by cellular substrates. A mechanism has been proposed recently in which the peptide, being positioned on the surface of the cell membrane, inhibits its fusion with the virus; the lipophilic chain of lipo-P59 is thought to insert into the membrane interior, thus anchoring the peptide at the surface. In the present work, lipid-peptide interactions of P59 and lipo-P59 with phospholipid liposomes are investigated using spin-label electron spin resonance spectroscopy. Two phospholipids have been examined, the zwitterionic dimyristoyl phosphatidylcholine and the anionic dimyristoyl phosphatidylglycerol, and a wide range of lipid spin labels, including positional isomers. Independent of the membrane charge, both peptides bind to lipid bilayers; however, whereas P59 insertion between the lipid headgroups leads to significant liposome destabilization, eventually resulting in vesicle fragmentation with the formation of smaller aggregates, lipo-P59 inserts with the lipophilic tail among the lipid chains, while the peptidic portion remains adsorbed onto the membrane, where it can effectively exert its antiviral activity.

Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes / D'Errico, Gerardino; A. M., D'Ursi; D., Marsh. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 47:(2008), pp. 5317-5327. [10.1021/bi7025062]

Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes.

D'ERRICO, GERARDINO;
2008

Abstract

P59, a 20-mer peptide modeled on the membrane-proximal external region (MPER) of the feline immunodeficiency virus (FIV) gp36 ectodomain, has potent antiviral activity. The lipoylated analogue, lipo-P59, displays a similar activity, which is preferentially retained by cellular substrates. A mechanism has been proposed recently in which the peptide, being positioned on the surface of the cell membrane, inhibits its fusion with the virus; the lipophilic chain of lipo-P59 is thought to insert into the membrane interior, thus anchoring the peptide at the surface. In the present work, lipid-peptide interactions of P59 and lipo-P59 with phospholipid liposomes are investigated using spin-label electron spin resonance spectroscopy. Two phospholipids have been examined, the zwitterionic dimyristoyl phosphatidylcholine and the anionic dimyristoyl phosphatidylglycerol, and a wide range of lipid spin labels, including positional isomers. Independent of the membrane charge, both peptides bind to lipid bilayers; however, whereas P59 insertion between the lipid headgroups leads to significant liposome destabilization, eventually resulting in vesicle fragmentation with the formation of smaller aggregates, lipo-P59 inserts with the lipophilic tail among the lipid chains, while the peptidic portion remains adsorbed onto the membrane, where it can effectively exert its antiviral activity.
2008
Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes / D'Errico, Gerardino; A. M., D'Ursi; D., Marsh. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 47:(2008), pp. 5317-5327. [10.1021/bi7025062]
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/336253
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 37
  • ???jsp.display-item.citation.isi??? 36
social impact