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Title [sv]
Stabiliserade försvarspeptider - ett nytt vapen i kampen mot infektioner. Proteinteknik av den humana försvarspeptiden LL-37.
Title [en]
Stable host defense peptides - novel weapons to battle infections. Bioengineering of the human host defense peptide LL-37.
Abstract [sv]
LL-37 is a human cathelicidin peptide with potent anti-bacterial and immunomodulatory activities. This project will exploit specific structural components of LL-37 that mediate antimicrobial activity, to improve potency and stability by using cyclic peptide analogues. The ultimate aim is to design a new chemical entity with improved pharmaceutical properties and potential as a new antibiotic agent. To achieve that goal we will use our combined expertise in peptide chemistry, biology and pharmaceutical sciences. Designed peptide analogues will be tested for membrane permeability, anti-bacterial activity, selectivity, stability and cytotoxicity. At the onset, we will systematically replace the individual amino acids in LL-37 by alanines and test these analogues to identify specific functional sites. The optimized peptide will then be used for the design of a cyclic peptide dimer. Active analogues will be characterized by NMR spectroscopy to extract detailed information on the three-dimensional structures necessary for bioactivity. The project has dual significance, as it will contribute towards both fundamental knowledge about antimicrobial peptides and their mode of action, besides providing a possible lead compound. In addition, the project addresses the fundamental question of stability of peptide and protein drugs. In specific, we will test the innovative concept of peptide cyclisation for stabilization.
Principal InvestigatorGöransson, Ulf
Coordinating organisation
Uppsala University
Funder
Period
2011-01-01 － 2013-12-31
National Category
Medicinal ChemistryMicrobiology in the medical areaMedical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
DiVA, id: project:4260Project, id: 2011-03403_VR
v. 2.47.0
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