Abstracts - faqs.org

Abstracts

Chemicals, plastics and rubber industries

Search abstracts:
Abstracts » Chemicals, plastics and rubber industries

Study of adsorption and penetration of E2(279-298) peptide into Langmuir phospholipid monolayers

Article Abstract:

A method to synthesize peptide corresponding to the sequence (279-298) of the Hepatitis G virus (HGV/GBV-C) E2 protein and surface activity measurements, pi-A compression isotherms, and penetration of E2 (279-298) into phospholipid monolayers spread at the air-water interface on the water and phosphate buffer subphases is presented. The observations show that the lipid acyl chain length is a significant factor to be considered in the study of peptide-lipid interactions.

Author: Alsina, M.A., Busquets, M.A., Trillo, J. Minones
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
Phosphates, Adsorption, Chemical synthesis

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Conductance of [alpha]-helical peptides trapped within molecular junctions

Article Abstract:

The investigation of mediated electron transfer was carried out by employing self-assembled monolayers of [alpha]-helical peptides on a gold surface. Measurements performed with peptides containing different numbers of amino acid residues indicate that the distance dependence of electron transmission through an [alpha]-helix is weaker than that through simple n-alkyl bridges.

Author: Sek, Slawomir, Misicka, Aleksandra, Swiatek, Karolina, Maicka, Elwira
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
Usage, Electron transport, Monomolecular films, Scanning tunneling microscopy

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Influence of the saturation chain and head group charge of phospholipids in the interaction of hepatitis G virus synthetic peptides

Article Abstract:

The properties at the air/water interface and the interaction of the hepatitis G virus synthetic peptide E1 and its palmitoyl with membrane phospholipids are studied using the Langmuir technique. The interaction is found to be influenced by the saturation of the acyl chain.

Author: Perez, S., Minonens, J., Jr., Espina, M., Alsina, M.A., Haro, I., Mestres, C.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
Peptide synthesis, Thin films, Multilayered, Multilayered thin films, Properties

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Chemical properties, Analysis, Peptides, Structure
Similar abstracts:
  • Abstracts: Molecular dynamics simulations of neutral chlorpromazine in zwitterionic phospholipid monolayers. Molecular-level control of the photoluminescence from PPV nanostructure films
  • Abstracts: String defects connecting pairs of half-integer disclinations and tilting transition of a Langmuir monolayer. Laser-induced local collapse in a Langmuir monolayer
  • Abstracts: Enthalpy changes upon dilution and ionization of poly(L-glutamic acid) in aqueous solutions. Cationic and anionic poly(N-isopropylacrylamide) based submicron gel particles: Electrokinetic properties and colloidal stability
  • Abstracts: Monte Carlo simulations of absorption and fluorescence spectra in ellipsoidal nanocavities. Conformational free energies of 1,2-dicloroethane in nanoconfined methanol
  • Abstracts: Effect of counterions on the interactions of charged oligothiophenes. Nonlinear infrared and optical responses of a Holstein-Peirls-Hubbard dimer
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.