New microviridins from a water bloom of the cyanobacterium Microcystis aeruginosa
Autor: | Shmuel Carmeli, Vered Reshef |
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Rok vydání: | 2006 |
Předmět: |
Serine protease
chemistry.chemical_classification Chromatography biology Stereochemistry Chemistry Organic Chemistry Absolute configuration Peptide General Medicine Mass spectrometry biology.organism_classification Biochemistry High-performance liquid chromatography Amino acid Drug Discovery Aspartic acid biology.protein Microcystis aeruginosa |
Zdroj: | Tetrahedron. 62:7361-7369 |
ISSN: | 0040-4020 |
DOI: | 10.1016/j.tet.2006.05.028 |
Popis: | Three new microviridins namely, SD1684 (1), SD1634 (2), and SD1652 (3), were isolated from the hydrophilic extract of Microcystis aeruginosa. The planar structures of compounds 1–3 were determined by homonuclear and inverse-heteronuclear 2D-NMR techniques as well as by high-resolution mass spectrometry. The absolute configuration of the asymmetric centers was studied using Marfey's method for HPLC. Compounds 1–3 contain l -threo-β-hydroxy aspartic acid as a building block of the peptide chain. This is the first example where microviridins contain non-proteinogenic amino acid in their structure. Compound 2 is a mild serine protease inhibitor. |
Databáze: | OpenAIRE |
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