Improvement of FGF7 Thermal Stability by Introduction of Mutations in Close Vicinity to Disulfide Bond and Surface Salt Bridge SCIE SCOPUS

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Title
Improvement of FGF7 Thermal Stability by Introduction of Mutations in Close Vicinity to Disulfide Bond and Surface Salt Bridge
Author(s)
An, Young Jun; Lee, Kyeong Won; Jung, Ye-Eun; Jeong, Ye Eun; Kim, Su-Jin; Woo, Jurang; Jin, Jonghwa; Lee, Won-Kyu; Cha, Kiweon; Cha, Sun-Shin; Lee, Jung Hyun; Yim, Hyung Soon
KIOST Author(s)
An, Young Jun(안영준)Lee, Kyeong Won(이경원)Lee, Jung Hyun(이정현)Yim, Hyung Soon(임형순)
Alternative Author(s)
안영준; 이경원; 이정현; 임형순
Publication Year
2022-03
Abstract
Fibroblast Growth Factor 7 (FGF7), a growth factor specific to epithelial cells, has attracted attention as a therapeutic protein. However, FGF7 has a limitation in its use due to low protein stability. Here, the mutations were designed to increase the stability of FGF7 by analyzing its 3D structure and sequence of other FGFs. Palifermin, N-terminal truncated FGF7 is known to have improved stability and was used as control protein in our study. The K126 and K178 were substituted into glutamate to form salt bridge with the neighboring residue R175 respectively and A120C mutation was introduced in close vicinity to disulfide bond between C133 and C137. The data of Circular Dichroism (CD) showed that all mutant proteins tested had higher Tm value than Palifermin and Tm of A120C/K126E/K178E FGF7 mutant protein was 15.24 degrees C higher than that of Palifermin. The results of cell proliferation activity and soluble protein analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) after 37 degrees C or 45 degrees C incubation exhibited that the stability of A120C mutant protein and A120C-including mutant proteins was improved. These results suggest that the mutation of amino acid in close vicinity to disulfide bond and the salt bridge at the surface of FGF7 enhanced thermal stability and make FGF7 more useful for pharmaceutical and cosmetical application.
ISSN
1573-3149
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/42425
DOI
10.1007/s10989-022-10394-1
Bibliographic Citation
International Journal of Peptide Research and Therapeutics, v.28, no.3, 2022
Publisher
Springer Verlag
Keywords
Salt bridge; Thermal stability; Fibroblast growth factor 7; KGF; FGF7
Type
Article
Language
English
Document Type
Article
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