Campus Units

Chemistry, Ames Laboratory

Document Type

Article

Publication Version

Published Version

Publication Date

6-2007

Journal or Book Title

Journal of the American Chemical Society

Volume

129

Issue

28

First Page

8845

Last Page

8849

DOI

10.1021/ja0719780

Abstract

An MCM-41-type mesoporous silica nanoparticle (MSN) material with a large average pore diameter (5.4 nm) is synthesized and characterized. The in vitro uptake and release profiles of cytochrome c by the MSN were investigated. The enzymatic activity of the released protein was quantitatively analyzed and compared with that of the native cytochrome c in physiological buffer solutions. We found that the enzymes released from the MSNs are still functional and highly active in catalyzing the oxidation of 2,2‘-azino-bis(3-ethylbenzthiazoline-6-sulfonate) (ABTS) by hydrogen peroxide. In contrast to the fact that cytochrome c is a cell-membrane-impermeable protein, we discovered that the cytochrome c-encapsulated MSNs could be internalized by live human cervical cancer cells (HeLa) and the protein could be released into the cytoplasm. We envision that these MSNs with large pores could serve as a transmembrane delivery vehicle for controlled release of membrane-impermeable proteins in live cells, which may lead to many important biotechnological applications including therapeutics and metabolic manipulation of cells.

Comments

Reprinted (adapted) with permission from Journal of the American Chemical Society 129 (2007): 8845, doi:10.1021/ja0719780. Copyright 2007 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

Included in

Chemistry Commons

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