TAILIEUCHUNG - Báo cáo khoa học: Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity

Host-derived anti-infective proteins represent an important source of sequences for designing antimicrobial peptides (AMPs). However such sequences are often long and comprise diverse amino acids with uncertain contribution to biological effects. Previously, we identified a simple highly cationic peptide derivative of human apolipoprotein E (apoEdp) that inhib-ited a range of microorganisms. | ỊFEBS Journal Apolipoprotein E-derived antimicrobial peptide analogues with altered membrane affinity and increased potency and breadth of activity Bridie A. Kelly1 Stuart J. Neil2 Aine McKnight2 t Joana M. Santos3 t Photini Sinnis3 Edward R. Jack1 David A. Middleton1 - and Curtis B. Dobson1 1 Faculty of Life Sciences The Mill The University of Manchester UK 2 WohlVirion Centre Windeyer Building University College London UK 3 Department of Medicaland Molecular Parasitology New York University Schoolof Medicine NY USA Keywords antimicrobialpeptides apolipoprotein E HIV Plasmodium membrane perturbation Correspondence C. B. Dobson Faculty of Life Sciences The Mill The University of Manchester PO Box 88 Sackville Street Manchester M60 1QD UK Fax 44 0 161 306 4433 Tel 44 0 161 306 8765 E-mail Present address Aaron Diamond AIDS Research Center New York NY USA tCentre for Infectious Disease Institute of Celland Molecular Science Barts and The London Queen Mary s Schoolof Medicine and Dentistry London UK Department of Microbiology and Molecular Medicine CMU University of Geneva Switzerland Division of StructuralBiology Department of Biologicalsciences University of Warwick Coventry UK -Schoolof BiologicalSciences University of Liverpool UK Received 4 May 2007 revised 22 June 2007 accepted 6 July 2007 Host-derived anti-infective proteins represent an important source of sequences for designing antimicrobial peptides AMPs . However such sequences are often long and comprise diverse amino acids with uncertain contribution to biological effects. Previously we identified a simple highly cationic peptide derivative of human apolipoprotein E apoEdp that inhibited a range of microorganisms. Here we have dissected the protein chemistry underlying this activity. We report that basic residues and peptide length of around 18 residues were required for activity however the Leu residues can be substituted by several other residues without loss of activity

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