Interaction study of peptide from VP3 capsid protein of hepatitis A virus through monolayers and fluorescence spectroscopy.
A synthetic peptide with the sequence [Lys113]VP3(110--121): FWRKDLVFDFQV, corresponding to an epitope of the VP3 capsid protein of hepatitis A virus (HAV), was synthesized by solid phase and characterized. To obtain insight into its physicochemical properties and to understand its possible mechanism of action at the membrane level, interaction with DPPC or DPPC/DPPG (95/5) liposomes and lipid monolayers of DPPC, DPPG, SA, PS, PA and SM were studied by fluorescence spectroscopy and Langmuir--Blotgett films technique, respectively. Fluorescence studies showed that the peptide was in a hydrophobic environment when DPPC liposomes were used. The addition of a 5% of a charged lipid, DPPG, to the preparations changed the preference of the peptide towards a polar surrounding. However, the peptide had a high surface activity (nmol/L) and was able to incorporate into lipid monolayers. Interaction was higher with charged phospholipids than with neutral ones. These results may have physiological significance in the mechanism of infection of host hepatic cells by HAV.
Sospedra
P
P
Physical Chemistry Department, Faculty of Pharmacy, University of Barcelona, Avgda Joan XXIII, s/n. 08028 Barcelona, Spain.
Prat
J
J
Haro
I
I
Mestres
C
C
Busquets
M A
MA
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry*; D006507:Hepatovirus / Q000737:chemistry*; D007700:Kinetics; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D010446:Peptide Fragments