Characterization of biomimetic surfaces formed from cell membranes.

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TitleCharacterization of biomimetic surfaces formed from cell membranes.
Publication TypeJournal Article
Year of Publication1997
AuthorsRao, NM, Plant, AL, Silin, VI, Wight, S, Hui, SW
JournalBiophys J
Volume73
Issue6
Pagination3066-77
Date Published1997 Dec
ISSN0006-3495
KeywordsAcetylcholinesterase, Animals, Biophysical Phenomena, Biophysics, Biosensing Techniques, Cell Membrane, Electrochemistry, Electron Transport, Erythrocyte Membrane, Gold, Humans, In Vitro Techniques, Liposomes, Microscopy, Atomic Force, Microscopy, Electron, Scanning, Rabbits, Surface Properties
Abstract

A method for fabricating biomimetic surfaces from intact cell membranes is described. A monolayer of alkanethiol on gold is covered by a second layer derived from the components of erythrocyte membranes either by self-assembly or by Langmuir-Blodgett methods. The resulting asymmetric hybrid layer was characterized by ellipsometry, surface plasmon resonance (SPR), contact angle, capacitance, voltammetry, and electron and atomic force microscopy. The erythrocyte membrane layer was measured to be approximately 30-40 A in thickness. Using SPR, the presence of erythrocyte components on the surface was demonstrated by their selective removal by enzymatic action. The uniform deposition of membranous material on the substrate was shown by electron and atomic force microscopy. Demonstration of acetylcholinesterase (AChase) activity, a membrane-anchored enzyme, on the surface for at least 8 days, suggests that the outer leaflet of the erythrocyte membrane is present in its native form. Cyclic voltammetry demonstrates that enhanced electron transport from a solution redox species accompanies formation of the erythrocyte layer at the surface. This enhanced electron transport is blocked by 4,4'-diisothiocyanate stilbene-2,2'-disulfonic acid, a well known blocker of anion transport, suggesting that an erythrocyte anion transporter protein is incorporated into the surface layer in an active conformation.

DOI10.1016/S0006-3495(97)78334-6
Alternate JournalBiophys. J.
PubMed ID9414220
PubMed Central IDPMC1181211
Grant ListGM 30969 / GM / NIGMS NIH HHS / United States