70-26-8Relevant articles and documents
Saccharochelins A-H, Cytotoxic Amphiphilic Siderophores from the Rare Marine Actinomycete Saccharothrix sp. D09
Bian, Xiaoying,Dai, Guangzhi,Jiao, Nianzhi,Liu, Yang,Ravichandran, Vinothkannan,Ren, Xiangmei,Shen, Qiyao,Sui, Haiyan,Zhang, Youming,Zhong, Lin,Zhou, Haibo
, p. 2149 - 2156 (2021/08/20)
Siderophores are secreted by microorganisms to survive in iron-depleted conditions, and they also possess tremendous therapeutic potential. Genomic-inspired isolation facilitated the identification of eight amphiphilic siderophores, saccharochelins A-H (1-8), from a rare marine-derived Saccharothrix species. Saccharochelins feature a series of fatty acyl groups appended to the same tetrapeptide skeleton. With the help of gene disruption and heterologous expression, we identified the saccharochelin biosynthetic pathway. The diversity of saccharochelins originates from the flexible specificity of the starter condensation (CS) domain at the beginning of the nonribosomal peptide synthetase (NRPS) toward various fatty acyl substrates. Saccharochelins showed cytotoxicity against several human tumor cell lines, with IC50 values ranging from 2.3 to 17 μM. Additionally, the fatty acid side chains of the saccharochelins remarkably affected the cytotoxicity, suggesting changing the N-terminal acyl groups of lipopeptides may be a promising approach to produce more potent derivatives.
COMBINING BETA-DIPEPTIDES AND AMINO ACIDS FOR OPTIMAL NUTRITIONAL SUPPLEMENTATION
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Page/Page column 10; 11, (2020/02/23)
The invention relates to anutritional supplement comprising a combination of one or more β-aspartyl-containing dipeptides,oroligomers thereof, or salts thereof, wherein each of the β-dipeptides comprises β-L-aspartyl as a first amino acid residue and an amino acid selected from arginine, lysine, ornithine, and citrulline as the second amino acid residue, and the respective second amino acid(s) or salts thereof. The invention further relates to the use of the combination for nutritional supplementation and to the combination for use in amino acid therapy.
Catenulobactins A and B, Heterocyclic Peptides from Culturing Catenuloplanes sp. with a Mycolic Acid-Containing Bacterium
Hoshino, Shotaro,Ozeki, Masahiro,Awakawa, Takayoshi,Morita, Hiroyuki,Onaka, Hiroyasu,Abe, Ikuro
supporting information, p. 2106 - 2110 (2018/09/12)
The production of two new heterocyclic peptide isomers, catenulobactins A (1) and B (2), in cultures of Catenuloplanes sp. RD067331 was significantly increased when it was cocultured with a mycolic acid-containing bacterium. The planar structures and absolute configurations of the catenulobactins were determined based on NMR/MS and chiral-phase GC-MS analyses. Catenulobactin B (2) displayed Fe(III)-chelating activity and moderate cytotoxicity against P388 murine leukemia cells.