Literature DB >> 27023356

PEGylation of cytochrome c at the level of lysine residues mediated by a microbial transglutaminase.

Jian Qin Zhou1, Ting He1, Jian Wen Wang2.   

Abstract

OBJECTIVES: To establish a method for microbial transglutaminase (mTG)-mediated PEGylation of proteins at the level of lysine (Lys) residues.
RESULTS: Carboxybenzyl-glutaminyl-glycinyl-methoxypolyethylene glycol (CBZ-QG-mPEG) was prepared by introducing carboxybenzyl-glutaminyl-glycine (CBZ-QG) to mPEG amine. The analysis by Fourier transform infrared spectroscopy and SDS-PAGE showed that CBZ-QG-mPEG was successfully synthesized and can be recognized by mTG as an acyl donor to modify therapeutic protein, cytochrome c (cyt c). Finally, under an optimized condition (cyt c 0.5 mg/ml, CBZ-QG-mPEG 11.25 mg/ml, mTG 0.5 mg/ml, 37 °C, 2 h), the PEGylation yield reached 76.5 %.
CONCLUSIONS: This is the first study regarding the PEGylation of protein at the level of Lys residues catalyzed by mTG. The novel method could be employed to immobilize active proteins and modify therapeutic proteins.

Entities:  

Keywords:  Lysine residue; Microbial transglutaminase; PEGylation; Therapeutic protein; Transglutaminase

Mesh:

Substances:

Year:  2016        PMID: 27023356     DOI: 10.1007/s10529-016-2083-6

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN: 0141-5492            Impact factor:   2.461


  2 in total

Review 1.  Review transglutaminases: part II-industrial applications in food, biotechnology, textiles and leather products.

Authors:  Lovaine Duarte; Carla Roberta Matte; Cristiano Valim Bizarro; Marco Antônio Záchia Ayub
Journal:  World J Microbiol Biotechnol       Date:  2019-12-26       Impact factor: 3.312

2.  Lysine-PEGylated Cytochrome C with Enhanced Shelf-Life Stability.

Authors:  João H P M Santos; Valker A Feitosa; Giovanna P Meneguetti; Gustavo Carretero; João A P Coutinho; Sónia P M Ventura; Carlota O Rangel-Yagui
Journal:  Biosensors (Basel)       Date:  2022-02-04
  2 in total

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