Interaction of arginine oligomer with model membrane.

نویسندگان

  • Dandan Yi
  • Li Guoming
  • Li Gao
  • Liang Wei
چکیده

Short oligomers of arginine (R8) have been shown to cross readily a variety of biological barriers. A hypothesis was put forward that inverted micelles form in biological membranes in the presence of arginine oligomer peptides, facilitating their transfer through the membranes. In order to define the role of peptide-lipid interaction in this mechanism, we prepared liposomes as the model membrane to study the ability of R8 inducing calcein release from liposomes, the fusion of liposomes, R8 binding to liposomes and membrane disturbing activity of the bound R8. The results show that R8 binding to liposome membrane depends on lipid compositions, negative surface charge density and interior water phase pH values of liposomes. R8 has no activity to induce the leakage of calcein from liposomes or improve liposome fusion. R8 does not permeabilize through the membrane spontaneously. These peptides delivering drugs through membranes may depend on receptors and energy.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Interaction of toxic and non-toxic HypF-N oligomers with lipid bilayers investigated at high resolution with atomic force microscopy

Protein misfolded oligomers are considered the most toxic species amongst those formed in the process of amyloid formation and the molecular basis of their toxicity, although not completely understood, is thought to originate from the interaction with the cellular membrane. Here, we sought to highlight the molecular determinants of oligomer-membrane interaction by atomic force microscopy. We mo...

متن کامل

Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure

Many proteins are transported across lipid membranes by protein translocation systems in living cells. The twin-arginine transport (Tat) system identified in bacteria and plant chloroplasts is a unique system that transports proteins across membranes in their fully-folded states. Up to date, the detailed molecular mechanism of this process remains largely unclear. The Escherichia coli Tat syste...

متن کامل

نقش نیتریک اکساید هسته مرکزی آمیگدال در بیان رفتار پاداشی مرفین در موش سفید بزرگ

Background and Objective: Naloxone shows interaction with the morphine in expression of reward behaviors. L-arginine increases morphine induced conditioned place preference, whereas L-NAME decreases this process. In this project, effects of injections of L-arginine and L-NAME intra-CeA on morphine induced drug-seeking behaviors including rearing, sniffing and compartment entering were investiga...

متن کامل

Determination of thermodynamic parameters of hydrogen permeation of palladium membrane for considering the effect of stainless steel support

A palladium composite membrane was prepared by electroless plating on oxidized porous stainless steel support (ox-PSS). Hydrogen permeation flux through this composite membrane was measured in the temperature range of 574-674K and the pressure difference of two sides of membrane up to 90kPa. A simplified resistance model was employed to analyze the permeation behavior of hydrogen through Pd/ox-...

متن کامل

In vivo experiments do not support the charge zipper model for Tat translocase assembly

The twin-arginine translocase (Tat) transports folded proteins across the bacterial cytoplasmic membrane and the plant thylakoid membrane. The Tat translocation site is formed by substrate-triggered oligomerization of the protein TatA. Walther and co-workers have proposed a structural model for the TatA oligomer in which TatA monomers self-assemble using electrostatic 'charge zippers' (Cell (20...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biochemical and biophysical research communications

دوره 359 4  شماره 

صفحات  -

تاریخ انتشار 2007