Scientific Publications - Work Done by Microbiology Reader Bioscreen C

Helena Hujakka, Jari Ratilainen, Timo Korjamo, Hilkka Lankinen, Pentti Kuusela, Harri Santa, Reino Laatikainen and Ale Närvänen,
Synthesis and antimicrobial activity of the symmetric dimeric form of temporin A based on 3-N,N-di(3-aminopropyl)amino propanoic acid as the branching unit, Bioorganic & Medicinal Chemistry, Volume 9, Issue 6, June 2001, Pages 1601-1607

ABSTRACT

Dimeric derivative of antimicrobial peptide amide Temporin A (TA) was synthesized by using a new branching unit 3-N,N-di(3-aminopropyl)amino propanoic acid (DAPPA), which allows building of the parallelly symmetric α-helical structures. Antimicrobial effect of the original peptide amide, its monomeric carboxy (TAc) and novel dimeric (TAd) analogues were tested against Staphylococcus aureus (Gram-positive) and Escherichia coli (Gram-negative). Both TA and TAd completely inhibited the growth of S. aureus at the concentrations of 5 and 10 µM, respectively, whereas TAc did not show any inhibitory activity. The activities of TAc, TA and TAd correlate directly with the net charges of the molecules, +1, +2 and +4, respectively. Interestingly, TAd displayed antibacterial effect against E. coli at a concentration of 10 µM, where as monomeric TA did not show any activity at concentration as high as 20 µM. The results indicate that the novel structural modification improves the antibacterial properties of Temporin A especially towards Gram-negative bacteria.

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Last modified: May 25, 2005