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Mirror image proteins.

Authors
  • Zhao, Le1
  • Lu, Wuyuan2
  • 1 First Affiliated Hospital, Xi'an Jiaotong University School of Medicine, China. , (China)
  • 2 Key Laboratory of Biomedical Information Engineering of the Ministry of Education, School of Life Science and Technology and Center for Translational Medicine, Frontier Institute of Science and Technology, Xi'an Jiaotong University, China; Institute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, USA. Electronic address: [email protected] , (China)
Type
Published Article
Journal
Current opinion in chemical biology
Publication Date
October 2014
Volume
22
Pages
56–61
Identifiers
DOI: 10.1016/j.cbpa.2014.09.019
PMID: 25282524
Source
Medline
License
Unknown

Abstract

Proteins composed entirely of unnatural d-amino acids and the achiral amino acid glycine are mirror image forms of their native l-protein counterparts. Recent advances in chemical protein synthesis afford unique and facile synthetic access to domain-sized mirror image d-proteins, enabling protein research to be conducted through 'the looking glass' and in a way previously unattainable. d-Proteins can facilitate structure determination of their native l-forms that are difficult to crystallize (racemic X-ray crystallography); d-proteins can serve as the bait for library screening to ultimately yield pharmacologically superior d-peptide/d-protein therapeutics (mirror-image phage display); d-proteins can also be used as a powerful mechanistic tool for probing molecular events in biology. This review examines recent progress in the application of mirror image proteins to structural biology, drug discovery, and immunology.

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