Structural highlights
Publication Abstract from PubMed
Two disulfide-containing peptides, barrettides A (1) and B (2), from the cold-water marine sponge Geodia barretti are described. Those 31 amino acid residue long peptides were sequenced using mass spectrometry methods and structurally characterized using NMR spectroscopy. The structure of 1 was confirmed by total synthesis using the solid-phase peptide synthesis approach that was developed. The two peptides were found to differ only at a single position in their sequence. The three-dimensional structure of 1 revealed that these peptides possess a unique fold consisting of a long beta-hairpin structure that is cross-braced by two disulfide bonds in a ladder-like arrangement. The peptides are amphipathic in nature with the hydrophobic and charged residues clustered on separate faces of the molecule. The barrettides were found not to inhibit the growth of either Escherichia coli or Staphylococcus aureus but displayed antifouling activity against barnacle larvae (Balanus improvisus) without lethal effects in the concentrations tested.
Isolation, Characterization, and Synthesis of the Barrettides: Disulfide-Containing Peptides from the Marine Sponge Geodia barretti.,Carstens BB, Rosengren KJ, Gunasekera S, Schempp S, Bohlin L, Dahlstrom M, Clark RJ, Goransson U J Nat Prod. 2015 Aug 28;78(8):1886-93. doi: 10.1021/acs.jnatprod.5b00210. Epub, 2015 Jul 29. PMID:26222779[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carstens BB, Rosengren KJ, Gunasekera S, Schempp S, Bohlin L, Dahlstrom M, Clark RJ, Goransson U. Isolation, Characterization, and Synthesis of the Barrettides: Disulfide-Containing Peptides from the Marine Sponge Geodia barretti. J Nat Prod. 2015 Aug 28;78(8):1886-93. doi: 10.1021/acs.jnatprod.5b00210. Epub, 2015 Jul 29. PMID:26222779 doi:http://dx.doi.org/10.1021/acs.jnatprod.5b00210
