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Engineering of erythrocyte-based drug carriers: control of protein release and bioactivity.

Summary of "Engineering of erythrocyte-based drug carriers: control of protein release and bioactivity."

This work reports the fabrication of layer-by-layer (LbL) polyelectrolyte coated erythrocyte carriers that provide a simple means for controlling the burst and subsequent release of lysozyme. Erythrocytes were loaded with RITC-lysozyme as model compound via the hypotonic dialysis method. An encapsulation efficiency of 41.6% and a loading amount of 12.7 pg/cell was achieved. It is demonstrated that these carriers maintain their shape and integrity similar to natural erythrocytes after the encapsulation procedures, and achieve a uniform distribution of the encapsulated lysozyme. The erythrocyte carriers were fixed with glutaraldehyde and then successfully coated with biocompatible polyelectrolytes, poly-
L:
-lysine hydrobromide and dextran sulfate, using the LbL method. It is demonstrated that the release profile of the encapsulated macromolecule can be regulated by adjusting the number of polyelectrolyte layers. Furthermore by adjusting the concentrations of the cross linking agent the activity of the encapsulated lysozyme can be well preserved. These core-shell microcapsules, consisting of erythrocytes loaded with bioactive substances and coated with a polyelectrolyte multilayer shell, hold promise for a new type of biocompatible and biodegradable drug delivery system.

Affiliation

School of Materials Science and Engineering, Nanyang Technological University, Block N4.1, Nanyang Avenue, Singapore, Singapore.

Journal Details

This article was published in the following journal.

Name: Journal of materials science. Materials in medicine
ISSN: 1573-4838
Pages:

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A ubiquitous membrane transport protein found in the plasma membrane of diverse cell types and tissues, and in nuclear, mitochondrial, and Golgi membranes. It is the major integral transmembrane protein of the erythrocyte plasma membrane, comprising 25% of the total membrane protein. It exists as a dimer and performs the important function of allowing the efficient transport of bicarbonate across erythrocyte cell membranes in exchange for chloride ion.

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