Structural and biological characterization of one antibacterial acylpolyamine isolated from the hemocytes of the spider Acanthocurria gomesiana
- Parasitology Department, Biomedical Sciences Institute, Sao Paulo University, Av Prof Lineu Prestes, 1374, 05508-900 Sao Paulo, SP (Brazil)
- Center for Applied Toxinology, Butantan Institute, Sao Paulo 05503-900 (Brazil)
- Biochemistry Department, Chemistry Institute, Sao Paulo University, Av Prof Lineu Prestes, 748, 05508-900 Sao Paulo, SP (Brazil)
- Okinawa Health Biotechnology Research Development Center, 12-75 Suzaki, Gushikawa, Okinawa 904-2234 (Japan)
We have isolated a 417 Da antibacterial molecule, named mygalin, from the hemocytes of the spider Acanthoscurria gomesiana. The structure of mygalin was elucidated by tandem mass spectrometry (MS/MS) and by two spectroscopic techniques, nuclear magnetic resonance (NMR) and ultraviolet (UV) spectroscopy. Mygalin was identified as bis-acylpolyamine N1,N8-bis(2,5-dihydroxybenzoyl)spermidine, in which the primary amino groups of the spermidine are acylated with the carboxyl group of the 2,5-dihydroxybenzoic acid. Mygalin was active against Escherichia coli at 85 {mu}M, being this activity inhibited completely by catalase. Therefore, the antibacterial activity of mygalin was attributed to its production of hydrogen peroxide (H{sub 2}O{sub 2}). The putative mechanisms of formation of H{sub 2}O{sub 2} from mygalin are discussed. To our knowledge this is the first report of one bis-acylpolyamine with antibacterial activity purified from animal source.
- OSTI ID:
- 20857975
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 352, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2006.11.128; PII: S0006-291X(06)02617-9; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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