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Expression of a fusion protein containing human epidermal growth factor and the collagen-binding domain of Vibrio mimicus metalloprotease
- Source :
- Biotechnology letters. 31(2)
- Publication Year :
- 2008
-
Abstract
- Human epidermal growth factor (hEGF) is a polypeptide of 53 amino acids, is an important autocrine/paracrine factor in the human body, and is used in the pharmaceutical and cosmetics industries. We constructed a fusion hEGF protein with a collagen-binding domain (CBD) composed of 33 amino acids from Vibrio mimicus metalloprotease (VMCBD). The CBD segment of the metalloprotease was fused at the C terminus of the hEGF protein. The recombinant fusion protein was expressed in Escherichia coli and purified. The purified hEGF protein promoted greater growth of human/A-431 cells than did the control hEGF. The fusion EGF protein also showed collagen-binding activity with type I collagen. In contrast, hEGF did not bind to type I collagen. These results suggest that recombinant hEGF protein fused to VMCBD may be able to remain for a long period at injured epidermal tissue acting as a healing agent.
- Subjects :
- Recombinant Fusion Proteins
Bioengineering
Biology
Protein Engineering
Applied Microbiology and Biotechnology
Epidermal growth factor
Escherichia coli
Humans
Autocrine signalling
chemistry.chemical_classification
Metalloproteinase
Binding Sites
Epidermal Growth Factor
General Medicine
Protein engineering
Fusion protein
Molecular biology
Amino acid
Protein Structure, Tertiary
Biochemistry
chemistry
Metalloproteases
Collagen
Vibrio mimicus
Type I collagen
Biotechnology
Binding domain
Protein Binding
Subjects
Details
- ISSN :
- 15736776
- Volume :
- 31
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biotechnology letters
- Accession number :
- edsair.doi.dedup.....715d16cab372fa5d0c2045cc5e97150e