Cited Article: Sokhan VP. Fluid flow in nanopores: Accurate boundary conditions for carbon nanotubes
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Title:
Towards mimicking natural protein channels with aligned carbon nanotube membranes for active drug delivery
Authors:
Majumder, M; Stinchcomb, A; Hinds, BJ
Author Full Names:
Majumder, Mainak; Stinchcomb, Audra; Hinds, Bruce J.
Source:
LIFE SCIENCES 86 (15-16): 563-568 APR 10 2010
Language:
English
Document Type:
Review
Author Keywords:
Drug delivery; Biomimetic; Nanostructure; Gatekeeper; Membrane; Transdermal; Nanoporous
KeyWords Plus:
WATER; TRANSPORT; POLYSTYRENE; GROWTH; FLOW
Abstract:
Aims: Carbon nanotube (CNT) membranes offer an exciting opportunity to mimic natural protein channels due to 1) a mechanism of dramatically enhanced fluid flow 2) ability to place 'gatekeeper' chemistry at the entrance to pores 3) the ability for biochemical reactions to occur on gatekeeper molecules and 4) an ability to chemically functionalize each side of the membrane independently.
Main methods: Aligned CNT membranes were fabricated and CNT pore entrances modified with gatekeeper chemistry. Pressure driven fluid flow and diffusion experiments were performed to study the mechanisms of transport through CNTs.
Key findings: The transport mechanism through CNT membranes is primarily 1) ionic diffusion near bulk expectation 2) gas flow enhanced 1-2 orders of magnitude primarily due to specular reflection 3) fluid flow 4-5 orders of magnitude faster than conventional materials due to a nearly ideal slip-boundary interface. The transport can be modulated by 'gatekeeper' chemistry at the pore entrance using steric hindrance, electrostatic attraction/repulsion, or biochemical state. The conformation of charged tethered molecules can be modulated by applied bias setting the stage for programmable drug release devices.
Significance: The membrane structure is mechanically far more robust than lipid bilayer films, allowing for large-scale chemical separations, delivery or sensing based on the principles of protein channels. The performance of protein channels is several orders of magnitude faster than conventional membrane materials. The fundamental requirements of mimicking protein channels are present in the CNT membrane system. Crown Copyright (C) 2009 Published by Elsevier Inc. All rights reserved.
Reprint Address:
Hinds, BJ, Univ Kentucky, Dept Chem & Mat Engn, Lexington, KY 40502 USA.
Research Institution addresses:
[Majumder, Mainak; Hinds, Bruce J.] Univ Kentucky, Dept Chem & Mat Engn, Lexington, KY 40502 USA; [Stinchcomb, Audra] Univ Kentucky, Coll Pharm, Lexington, KY 40502 USA
E-mail Address:
bjhinds@engr.uky.edu
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Cited Reference Count:
33
Times Cited:
1
Publisher:
PERGAMON-ELSEVIER SCIENCE LTD; THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
Subject Category:
Medicine, Research & Experimental; Pharmacology & Pharmacy
ISSN:
0024-3205
DOI:
10.1016/j.lfs.2009.04.006
IDS Number:
581UY
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