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Expression and characterization of recombinant rattusin, an α-defensin-related peptide with a homodimeric scaffold formed by intermolecular disulfide exchanges.

Authors
  • Ji, Sehyeon1
  • Yun, Hyosuk1
  • Park, Gwansik1
  • Min, Hye Jung2
  • Lee, Chul Won3
  • 1 Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea. , (North Korea)
  • 2 Department of Pharmaceutical Cosmetics, Kwangju Women's University, Gwangju 62396, Republic of Korea. Electronic address: [email protected] , (North Korea)
  • 3 Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea. Electronic address: [email protected] , (North Korea)
Type
Published Article
Journal
Protein Expression and Purification
Publisher
Elsevier
Publication Date
Jul 01, 2018
Volume
147
Pages
17–21
Identifiers
DOI: 10.1016/j.pep.2018.02.006
PMID: 29454031
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

Rattusin is an α-defensin-related peptide isolated from the small intestine of rats. The primary sequence of linear rattusin is composed of 31 amino acids containing five cysteines with a unique spacing pattern. It forms a homodimeric scaffold in which the primary structure occurs in an antiparallel fashion formed by five intermolecular disulfide (SS) bonds. Rattusin is a highly potent antibiotic, which not only exhibits broad-spectrum antimicrobial activity, but also maintains its antimicrobial activity at physiological salt concentrations. Therefore, to develop new antibiotics based on rattusin, structural and functional studies of rattusin should be performed. For this purpose, large amounts of linear rattusin precursor must be obtained through appropriate preparation methods. Therefore, we established a mass production technique for linear rattusin by using recombinant protein expression and purification procedures. We verified that structure and activity of the recombinant rattusin are identical to the chemically synthesized rattusin. The described method for producing recombinant rattusin provides a high yield of rattusin, which can be used to study the biochemical and functional properties of rattusin and for the development of rattusin-based peptide antibiotics. Copyright © 2018 Elsevier Inc. All rights reserved.

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