Efficient encapsulation of functional proteins into erythrocytes by controlled shear-mediated membrane deformation. Issue 11 (18th May 2021)

• Record Type: Journal Article
• Authors: Rahman, Md Habibur; Wong, Chung Hong Nathaniel; Lee, Marianne M.; Chan, Michael K.; Ho, Yi-Ping
• Is Part Of: Lab on a chip. Volume 21:Issue 11(2021)
• Page Start: 2121
• Page End: 2128
• Publication Date: 2021-05-18
• Subjects: Miniature electronic equipment -- Periodicals; Combinatorial chemistry -- Periodicals; Biotechnology -- Periodicals; 543.0813
• DOI: 10.1039/d0lc01077d
• Languages: English
• ISSNs: 1473-0197

Abstract

Abstract : This work demonstrates an investigation to deliver proteins and enzymes to red blood cells (RBCs) by shear-mediated membrane deformation in physiological buffers, which is expected to bridge the gap between enzyme- and RBC-mediated therapies. Abstract : Red blood cells (RBCs) are attractive carriers of biomolecular payloads due to their biocompatibility and the ability to shelter their encapsulated cargo. Commonly employed strategies to encapsulate payloads into RBCs, such as hypotonic shock, membrane fusion or electroporation, often suffer from low throughput and unrecoverable membrane impairment. This work describes an investigation of a method to encapsulate protein payloads into RBCs by controlling membrane deformation either transiently or extendedly in a microfluidic channel. Under the optimized conditions, the loading efficiency of enhanced green fluorescent protein into mouse RBCs increased was about 2.5- and 4-fold compared to that with osmotic entrapment using transient and extended deformation, respectively. Significantly, mouse RBCs loaded with human arginase exhibit higher enzymatic activity and membrane integrity compared to their counterparts loaded by osmotic entrapment. These features together with the fact that this shear-mediated encapsulation strategy allows loading with physiological buffers highlight the key advantages of this approach compared to traditional osmotic entrapment.