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Upstream product

• 29475-64-7 N-methyl-D-alanine 
• 95713-52-3 N-(2,4-dinitro-5-fluorophenyl)-L-alaninamide 
• 600-21-5 N-methylalanine 

Relevant academic research and scientific papers

Friomaramide, a Highly Modified Linear Hexapeptide from an Antarctic Sponge, Inhibits Plasmodium falciparum Liver-Stage Development

The cold waters of Antarctica are known to harbor a rich biodiversity. Our continuing interest in the chemical analysis of Antarctic invertebrates has resulted in the isolation of friomaramide (1), a new, highly modified hexapeptide, from the Antarctic sponge Inflatella coelosphaeroides. The structure of friomaramide was determined using spectroscopic methods and its configuration established by Marfey's method. Friomaramide, which bears the unusual permethylation of the amino acid backbone and is the longest polypeptide bearing a tryptenamine C-terminus, blocks >90% of Plasmodium falciparum liver-stage parasite development at 6.1 μM.

Odoamide, a cytotoxic cyclodepsipeptide from the marine cyanobacterium Okeania sp.

The bioassay-guided fractionation of the Okinawan marine cyanobacterium Okeania sp. led to the isolation of the 26-membered cyclodepsipeptide odoamide (1). The gross structure of 1 was determined by 1D and 2D NMR analyses, whereas its absolute stereochemistry was determined using a variety of different methods, including synthesis and chemical degradation followed by chiral HPLC analysis. Notably, odoamide (1) showed potent cytotoxicity against HeLa S3 human cervical cancer cells with an IC50value of 26.3?nM.

Jahanyne, an apoptosis-inducing lipopeptide from the marine cyanobacterium lyngbya sp.

An acetylene-containing lipopeptide, jahanyne, was isolated from the marine cyanobacterium Lyngbya sp. Its gross structure was established by spectroscopic analyses, and the absolute configuration was clarified based on a combination of chiral HPLC analyses, spectroscopic analyses, and derivatization reactions. Jahanyne significantly inhibited the growth of human cancer cells and induced apoptosis in HeLa cells.

Psychrophilins E-H and versicotide C, cyclic peptides from the marine-derived fungus aspergillus versicolor ZLN-60

Four new cyclic peptides, psychrophilins E-H (1-4), possessing a rare amide linkage between the carboxylic acid in anthranilic acid (ATA) and the nitrogen from an indole moiety, along with a new ATA-containing hexapeptide, versicotide C (5), were obtained from the culture of the marine-derived fungus Aspergillus versicolor ZLN-60. The structures, including absolute configurations, were elucidated by a combination of HRESIMS, NMR, X-ray crystallography, TDDFT ECD calculations, and Marfeys method. Versicotide C (5) is the first natural cyclic hexapeptide containing two anthranilic acids. Compounds 1-5 were not cytotoxic, and compound 3 showed potent lipid-lowering effects.

Two new cyclic pentapeptides from the marine-derived fungus aspergillus versicolor

Two new cyclic pentapeptides, named versicotides A (1) and B (2), were obtained from a marine-derived fungus strain ZLN-60, identified as Aspergillus versicolor. Their structures were established on the basis of chemical and spectroscopic evidence. Versic

Evolved diversification of a modular natural product pathway: Apratoxins F and G, two cytotoxic cyclic depsipeptides from a palmyra collection of Lyngbya bouillonii

A collection of Lyngbya bouillonii from Palmyra Atoll in the Central Pacific, a site several thousand kilometers distant from all previous collections of this chemically prolific species of cyanobacterium, was found to contain two new cancer cell cytotoxins of the apratoxin family. The structures of the new compounds, apratoxins F and G, were determined by 1D and 2D NMR techniques in combination with mass spectrometric methods. Stereochemistry was explored by using chromatographic analyses of the hydrolytically released fragments in combination with NMR and optical rotation comparisons with known members of the apratoxin family. Apratoxins F and G add fresh insights into the SAR of this family because they incorporate an N-methyl alanine residue at a position where all prior apratoxins have possessed a proline unit, yet they retain high potency as cytotoxins to H-460 cancer cells with IC50 values of 2 and 14 nM, respectively. Additional assays using zone inhibition of cancer cells and clonogenic cells give a comparison of the activities of apratoxin F to apratoxin A. Additionally, the clonogenic studies in combination with maximum tolerated dose (MTD) studies provided insights as to dosing schedules that should be used for in vivo studies, and preliminary in vivo evaluation validated the predicted in vivo efficacy for apratoxin A. These new apratoxins are illustrative of a mechanism (the modification of an NRPS adenylation domain specificity pocket) for evolving a biosynthetic pathway so as to diversify the suite of expressed secondary metabolites.