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Current Topics in Peptide & Protein Research   Volumes    Volume 24 
Two N-terminally derived and expressed fatty acid-binding peptides of DUF538
Ashraf Gholizadeh
Pages: 41 - 48
Number of pages: 8
Current Topics in Peptide & Protein Research
Volume 24 

Copyright © 2023 Research Trends. All rights reserved

The fatty acid-binding ability of DUF538 (domain of unknown function 538) protein family in plants was predicted by using molecular docking bioinformatics tools. Two N-terminally derived and engineered peptides (peptide1: KWLVNKIK GKMQ; peptide2: PSICEVGYKDSSVLKFTTKT KVMIWVK) were identified to be the fatty acid-binding elements of DUF538. Using His tag-based recombinant technology, the heterogeneous expression and production of the predicted binding peptides were successfully examined and reported in Escherichia coli cells without affecting the recombinant bacterial cell growth. The recombinant extracts containing peptide1 and peptide2 fusion products exhibited palmitic acid-binding abilities of about 64% and 28%, respectively. As a first report, the presently studied peptides were introduced as novel fatty acid-binding peptides that may be used in medical biotechnology and drug development. 
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