Macromolecular structures represent an interesting starting point for the design and synthesis of small-molecule mimetics of surface epitopes that mediate protein–protein and protein–nucleic acid interactions. The resulting protein epitope mimetics (PEMs) provide a source
of new biologically active molecules that are useful as biomolecular probes in chemical biology, as well as novel drug or vaccine candidates. This is illustrated here through studies on PEMs as synthetic vaccine candidates targeting the malaria parasite and the human immunodeficiency virus
type-1 (HIV-1). In addition, various folded PEMs with β-hairpin structures have been designed that target protein–protein and protein–nucleic acid interactions, as well as others that interact with cellular receptors such as CXCR4 and the bacterial outer membrane protein LptD.
In this last example, the PEMs possess a novel antibiotic activity that has so far not been observed with traditional small synthetic molecules or natural products.
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PROTEIN EPITOPE MIMETICS;
Document Type: Research Article
Chemistry Department, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
Publication date: December 1, 2013
More about this publication?
International Journal for Chemistry and Official Membership Journal of the Swiss Chemical Society (SCS) and its Divisions
CHIMIA, a scientific journal for chemistry in the broadest sense, is published 10 times a year and covers the interests of a wide and diverse readership. Contributions from all fields of chemistry and related areas are considered for publication in the form of Review Articles and Notes. A characteristic feature of CHIMIA are the thematic issues, each devoted to an area of great current significance.
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