Synthesis, Structural Characterization, and Bioactivity of the Stable Peptide RCB-1 from Ricinus communis
2015 (English)In: Journal of natural products (Print), ISSN 0163-3864, E-ISSN 1520-6025, Vol. 78, no 11, 2545-2551 p.Article in journal (Refereed) PublishedText
The Ricinus communis biomarker peptides RCB-1 to -3 comprise homologous sequences of 19 (RCB-1) or 18 (RCB-2 and -3) amino acid residues. They all include four cysteine moieties, which form two disulfide bonds. However, neither the 3D structure nor the biological activity of any of these peptides is known. The synthesis of RCB-1, using microwave-assisted, Fmoc-based solid-phase peptide synthesis, and a method for its oxidative folding are reported. The tertiary structure of RCB-1, subsequently established using solution-state NMR, reveals a twisted loop fold with antiparallel ?-sheets reinforced by the two disulfide bonds. Moreover, RCB-1 was tested for antibacterial, antifungal, and cytotoxic activity, as well as in a serum stability assay, in which it proved to be remarkably stable.
Place, publisher, year, edition, pages
2015. Vol. 78, no 11, 2545-2551 p.
IdentifiersURN: urn:nbn:se:uu:diva-272306DOI: 10.1021/acs.jnatprod.5b00463ISI: 000366005800005PubMedID: 26509914OAI: oai:DiVA.org:uu-272306DiVA: diva2:894161
FunderSwedish Research Council, 621-2007-567Swedish Foundation for Strategic Research , F06-0058