194852-51-2

Upstream product

• 56-87-1 L-lysine 
• 95713-52-3 N-(2,4-dinitro-5-fluorophenyl)-L-alaninamide 
• 1435677-74-9 sungsanpin 
• 1241376-50-0 sagittamide E 
• 1232889-36-9 sclerotiotide C 

Relevant academic research and scientific papers

Cyclic tripeptides from the halotolerant fungus Aspergillus sclerotiorum PT06-1

Eleven new aspochracin-type cyclic tripeptides, sclerotiotides A-K (1-11), together with three known compounds, JBIR-15 (12), aspochracin (13), and penicillic acid, were isolated from the ethyl acetate extract of the fermentation broth of the halotolerant Aspergillus sclerotiorum PT06-1 in a hypersaline nutrient-rich medium. Their structures were elucidated by spectroscopic analysis and chemical methods. Chemical transformations of 12 and 13 proved that sclerotiotides D-K (4-11) were artifacts probably formed during the fermentation or subsequent isolation steps. All 13 cyclic tripeptides have been evaluated for their antimicrobial and cytotoxic effects. Only sclerotiotides A (1), B (2), F (6), and I (9) and JBIR-15 (12) showed selective antifungal activity against Candida albicans with MIC values of 7.5, 3.8, 30, 6.7, and 30 μM, respectively.

Stereochemical elucidation of new sagittamides CF from a didemnid ascidian

Four new minor congeners, sagittamides CF, were isolated from an unidentified Didemnid tunicate that previously afforded sagittamides A and B. The structures were determined by interpretation of spectroscopic data, degradation to amino acids, and comparisons with sagittamide A. An unexpected change in relative configuration of the hexacetoxy C5C10 stereoelement is present in sagittamides D and F. A tentative assignment of configuration was possible through a systematic deduction based on analysis of 13C NMR data and symmetry considerations.

C3 and 2D C3 Marfey's Methods for Amino Acid Analysis in Natural Products

We validate the improved resolution and sensitivity of the C3 Marfey's method, including an ability to resolve all Ile isomers, against an array of amino acids commonly encountered in natural products and by comparison to an existing Marfey's m

Sungsanpin, a lasso peptide from a deep-sea streptomycete

Sungsanpin (1), a new 15-amino-acid peptide, was discovered from a Streptomyces species isolated from deep-sea sediment collected off Jeju Island, Korea. The planar structure of 1 was determined by 1D and 2D NMR spectroscopy, mass spectrometry, and UV spectroscopy. The absolute configurations of the stereocenters in this compound were assigned by derivatizations of the hydrolysate of 1 with Marfey's reagents and 2,3,4,6-tetra-O-acetyl-β-d- glucopyranosyl isothiocyanate, followed by LC-MS analysis. Careful analysis of the ROESY NMR spectrum and three-dimensional structure calculations revealed that sungsanpin possesses the features of a lasso peptide: eight amino acids (-Gly1-Phe-Gly-Ser-Lys-Pro-Ile-Asp8-) that form a cyclic peptide and seven amino acids (-Ser9-Phe-Gly-Leu-Ser-Trp-Leu 15) that form a tail that loops through the ring. Sungsanpin is thus the first example of a lasso peptide isolated from a marine-derived microorganism. Sungsanpin displayed inhibitory activity in a cell invasion assay with the human lung cancer cell line A549.