Abstract
The extract of UIC 10035, a strain obtained from a sample collected near the town of Homestead, South Florida, showed antiproliferative activity against MDA-MB-435 cells. Bioassay-guided fractionation led to the isolation of a series of cyclic lipodecapeptides, named minutissamides E–L (1–8). The planar structures were determined by analysis of HRESIMS, tandem MS, and 1D and 2D NMR data, and the stereoconfigurations were assigned by LC–MS analysis of the Marfey’s derivatives after acid hydrolysis. Minutissamides E–L (1–8) exhibited antiproliferative activity against MDA-MB-435 cells with IC50 values ranging between 1 and 10μM. The structures of minutissamides E–L (1–8) were closely related with those of the previously reported lipopeptides, puwainaphycins A–E and minutissamides A–D, characterized by the presence of a lipophilic β-amino acid and three non-standard amino acids NMeAsn, OMeThr and Dhb (α,β-dehydro-α-aminobutyric acid). The strain UIC 10035 was designated as cf. Anabaena sp. on the basis of morphological and 16S rRNA gene sequence analyses.
Highlights
This subset of nonribosomal peptides has shown a wide range of biological activities including antibacterial and antifungal as well as cytotoxic activities, and some of these cyclic lipopeptides are regarded as promising candidates for clinical evaluation
The elevated concentration of intracellular Ca2+ and subsequent cell necrosis were observed upon addition of puwainaphycins F/G, indicating that these cyanobacterial lipopeptides interact with cell membrane, causing membrane depolarization in a similar manner to the well-known pore-forming lipopeptides, such as daptomycin and syringomycin
We recently reported four cyclic lipodecapeptides, named minutissamides A - D, possessing a ipophilic -amino acid residue and the nonstandard amino acids NMeAsn and Dhb, from the cultured cyanobacterium Anabaena minutissima UTEX 1613.14 we report the isolation, structure determination and biological activity of an additional set of cyclic lipodecapeptides, named minutissamides E - L (1 – 8) due to the structural similarity to the previously reported minutissamides A - D
Summary
Cyclic lipopeptides represent a large subclass of non-ribosomal peptides, which often contain non-standard amino acids such as Dhb (, -dehydro- -aminobutyric acid), hydroxylated amino acids, and N- and/or O-methylated amino acids. This subset of nonribosomal peptides has shown a wide range of biological activities including antibacterial and antifungal as well as cytotoxic activities, and some of these cyclic lipopeptides are regarded as promising candidates for clinical evaluation. Mode of action studies of the phytotoxin syringomycin from Pseudomonas syringae and the antibiotic daptomycin from Streptomyces roseosporus indicated that their lipophilic residues play key roles for the biological activities of these molecules. The presence of lipophilic residues allows these. Cyclic lipopeptides represent a large subclass of non-ribosomal peptides, which often contain non-standard amino acids such as Dhb (, -dehydro- -aminobutyric acid), hydroxylated amino acids, and N- and/or O-methylated amino acids. . Cyclic lipopeptides represent a large subclass of non-ribosomal peptides, which often contain non-standard amino acids such as Dhb (, -dehydro- -aminobutyric acid), hydroxylated amino acids, and N- and/or O-methylated amino acids.1, 2 This subset of nonribosomal peptides has shown a wide range of biological activities including antibacterial and antifungal as well as cytotoxic activities, and some of these cyclic lipopeptides are regarded as promising candidates for clinical evaluation.. The elevated concentration of intracellular Ca2+ and subsequent cell necrosis were observed upon addition of puwainaphycins F/G, indicating that these cyanobacterial lipopeptides interact with cell membrane, causing membrane depolarization in a similar manner to the well-known pore-forming lipopeptides, such as daptomycin and syringomycin. Minutissamides E - L (1 – 8) featured cyclic lipodecapeptide architectures characterized by the presence of one lipophilic -amino acid (octadecanoic or tetradecanoic acids) with 3-amino-2-hydroxy-4methyl functionality, and three non-standard amino acids NMeAsn, OMeThr and Dhb
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