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BIO DESIGN

pISSN 2288-6982
eISSN 2288-7105

Article

Article

Article

BioDesign 2024; 12(3): 39-43

Published online September 30, 2024

https://doi.org/10.34184/kssb.2024.12.3.39

© Korean Society for Structural Biology

MBP fusion proteins: enhanced expression and solubility, unexpected cleavage dilemma

Cheolwoo Jeong1,2 and Hyo Jung Kim1,2,*

1College of Pharmacy, Woosuk University, Wanju 55338, Republic of Korea
2Research Institute of Pharmaceutical Sciences, Woosuk University, Wanju 55338, Republic of Korea

Correspondence to: *hyojungkim@woosuk.ac.kr

Received: July 1, 2024; Accepted: September 1, 2024

Abstract

Protein isolation and purification are critical steps in protein research involving recombinant DNA technology. Numerous techniques have been developed to optimize these processes for efficiency. Escherichia coli is the most common expression host for recombinant protein production; however, low expression levels or solubility often pose challenges for subsequent steps. To address this issue, target proteins are frequently linked with large tags, such as maltose binding protein (MBP). In this study, we present two examples of improved characteristics observed after incorporating MBP into target proteins. However, during the crystallization process, the MBP tag undergoes unexpected autocleavage in many forms of MBP fusion protein crystals. Our study highlights MBP as a beneficial tag for enhancing protein characteristics, though careful engineering of the linker sequence is necessary for selective cleavage of MBP fusion proteins.