Unique Polyhalogenated Peptides from the Marine Sponge sp.
Rogelio Fernández, Asep Bayu, Tri Aryono Hadi, Santiago Bueno, Marta Pérez, Carmen Cuevas, Masteria Yunovilsa Putra
Author Information
Rogelio Fernández: Natural Products Department, PharmaMar S.A., Pol. Ind. La Mina Norte, Avda. de los Reyes 1, 28770 Colmenar Viejo (Madrid), Spain.
Asep Bayu: Research Center for Biotechnology, Indonesian Institute of Sciences, Jl. Raya Jakarta-Bogor No. Km46, Cibinong, Bogor, Jawa Barat 16911, Indonesia.
Tri Aryono Hadi: Research Center for Oceanography, Indonesian Institute of Sciences, Jl. Pasir Putih I, Ancol Timur, Jakarta 14430, Indonesia.
Santiago Bueno: Natural Products Department, PharmaMar S.A., Pol. Ind. La Mina Norte, Avda. de los Reyes 1, 28770 Colmenar Viejo (Madrid), Spain.
Marta Pérez: Natural Products Department, PharmaMar S.A., Pol. Ind. La Mina Norte, Avda. de los Reyes 1, 28770 Colmenar Viejo (Madrid), Spain. ORCID
Carmen Cuevas: Natural Products Department, PharmaMar S.A., Pol. Ind. La Mina Norte, Avda. de los Reyes 1, 28770 Colmenar Viejo (Madrid), Spain.
Masteria Yunovilsa Putra: Research Center for Biotechnology, Indonesian Institute of Sciences, Jl. Raya Jakarta-Bogor No. Km46, Cibinong, Bogor, Jawa Barat 16911, Indonesia. ORCID
Two new bromopyrrole peptides, haloirciniamide A () and seribunamide A (), have been isolated from an Indonesian marine sponge of the genus collected in the Thousand Islands (Indonesia). The planar structure of both compounds was assigned on the basis of extensive 1D and 2D NMR spectroscopy and mass spectrometry. The absolute configuration of the amino acid residues in and was determined by the application of Marfey's method. Compound is the first dibromopyrrole cyclopeptide having a chlorohistidine ring, while compound is a rare peptide possessing a tribromopyrrole ring. Both compounds failed to show significant cytotoxicity against four human tumor cell lines, and neither compound was able to inhibit the enzyme topoisomerase I or impair the interaction between programmed cell death protein PD1 and its ligand, PDL1.
