Expression, purification and characterization of TAT-high mobility group box-1A peptide as a carrier of nucleic acids
- Authors
- Kim, Kyunghwa; Han, Jee Seung; Kim, Hyun Ah; Lee, Minhyung
- Issue Date
- Aug-2008
- Publisher
- SPRINGER
- Keywords
- gene delivery; high mobility group box 1; peptide; purification; transfection
- Citation
- BIOTECHNOLOGY LETTERS, v.30, no.8, pp.1331 - 1337
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOTECHNOLOGY LETTERS
- Volume
- 30
- Number
- 8
- Start Page
- 1331
- End Page
- 1337
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/171922
- DOI
- 10.1007/s10529-008-9695-4
- ISSN
- 0141-5492
- Abstract
- High mobility group box 1 (HMGB1) is an abundant nuclear protein that binds to double-stranded DNA. HMGB1 is composed of high mobility (HMG) box A, box B, and C-terminal acidic regions. In this study, a recombinant TAT linked HMGB1 box A (rTAT-HMGB1A) peptide was expressed, purified, and characterized as a carrier of nucleic acids. The HMGB1A cDNA was amplified by PCR, and cloned into the pET21a expression vector with the TAT domain located at the N-terminus. The rTAT-HMGB1A peptide was overexpressed and purified using Nickel affinity chromatography. A recombinant HMGB1A (rHMGB1A) peptide without the TAT domain was also overexpressed and purified as a control. In gel retardation assays, both the rHMGB1A and rTAT-HMGB1A peptides formed complexes with DNA equally well. However, transfection assays showed that the rTAT-HMGB1A peptide had a higher gene transfer efficiency than rHMGB1A. Finally, rTAT-HMGB1A had no cytotoxicity to HEK 293 cells suggesting that rTAT-HMGB1A may be useful as a non-toxic gene delivery carrier.
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