Corrigendum to “Depsipeptides from a Guamanian Marine Cyanobacterium, Lyngbya bouillonii, with Selective Inhibition of Serine Proteases” [Tetrahedron Letters 51 (2010) 6718–6721]

Rubio, Brent K.; Parrish, Stephen M.; Yoshida, Wesley Y.; Schupp, Peter J.; Schils, Tom; Williams, Philip G.

doi:10.1016/j.tetlet.2012.03.020

Cited by 2 publications

(3 citation statements)

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“…12aII (120 mg) was further purified by preparative HPLC using 20% aqueous CH 3 CN (0.1% formic acid), to obtain Determination of Absolute Configurations of Ahp/Amp and Mpc Units. Compounds 1, 2, and 4 (0.5 mg each) were oxidized by Jones' reagent 26 (1.5 mL of H 2 O with 3 mg K 2 Cr 2 O 7 , to which 3 mL of 67% aqueous H 2 SO 4 was added dropwise at 0 °C). The mixture was stirred and allowed to warm to room temperature over 5 h, then extracted with CH 2 Cl 2.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

“…Three serine proteases including elastase, chymotrypsin, and trypsin inhibitory activities were evaluated according to the method as previously described. 26 Elastase inhibition was determined using porcine pancreatic elastase (Sigma E0258) and N-succinyl-Ala-Ala-Ala-p-nitroanilide (Sigma S4760) as a substrate. Next, 79 μL of buffer (1.0 M Tris-HCl (pH 8.0)), 1 μL of compound (5-fold dilution in DMSO from 10 mM to 0.016 mM), and 5 μL of elastase solution (75 μg/mL in assay buffer) were mixed and added to each well of 96-well plate.…”

Section: ■ Experimental Sectionmentioning

confidence: 99%

“…25) nm; 1 H and13 C NMR data, see Table2; HRESIMS m/z 1004.4729 [M − H] − (calcd for C 49 H 66 N 9 O 14 , 1004.4729).Determination of Absolute Configurations of Amino Acid Residues. The absolute configurations of 1−4 were assigned by advanced Marfey's method13,26 after hydrolysis. Compounds 1−4 (0.5 mg each) were hydrolyzed in 6 N HCl (1 mL) at 110 °C for 16 h in a sealed thick tube.…”

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Dinghupeptins A–D, Chymotrypsin Inhibitory Cyclodepsipeptides Produced by a Soil-Derived Streptomyces

et al. 2018

J. Nat. Prod.

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Four new cyclodepsipeptides, dinghupeptins A-D (1-4), possessing a rare N-(2-hydroxylethyl)glutamine moiety, were isolated from cultures of the soil-derived Streptomyces sp. SC0581. Their structures were elucidated by spectroscopic and advanced Marfey's amino acid analysis, and their 3D structures were established by theoretical conformational analysis. Compounds 1 and 2, containing a 3-amino-6-hydroxypiperidone unit, displayed selective inhibition of chymotrypsin with IC values of 2.1 and 1.1 μM, respectively. Enzyme kinetic analysis and molecular docking experiments revealed they are competitive inhibitors binding to the active site of chymotrypsin.

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Section: ■ Experimental Sectionmentioning

confidence: 99%

Section: ■ Experimental Sectionmentioning

confidence: 99%

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confidence: 99%

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Dinghupeptins A–D, Chymotrypsin Inhibitory Cyclodepsipeptides Produced by a Soil-Derived Streptomyces

et al. 2018

J. Nat. Prod.

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Carotenoid Profile of Freshwater Microalgae Mychonastes racemosus AUP1 and its Antioxidant properties

Kusnanda

Dharma

Armaini

et al. 2023

RJPT

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Microalgae contain some active compounds that can be used for various purposes, such as carotenoids and high-value compounds with antioxidant capacity to be used as ingredients for food and pharmaceuticals This study aims to isolate microalgae from freshwater to produce carotenoid pigments. A green microalga was isolated from a local freshwater pond. Morphological observation and molecular analysis were performed to identify the microalgae. The molecular phylogenetic analysis was conducted based on the sequences of 18S rRNA genes. The carotenoid pigments were then extracted from the microalgae using water: methanol: dichloromethane (1:2:1,v/v/v). Further carotenoid pigments were then characterized using ultraviolet–visible (UV–Vis) spectrophotometry, FTIR, and HPLC. The antioxidant activity of the microalgae carotenoid extracts was determined with the 2,2-diphenyl-2-picrylhydrazyl hydrate (DPPH) radical scavenging assay. The results showed that the microalgae belong to the species Mychonastes racemosus AUP1. Carotenoid extracts was obtained from microalgae were about to 86 mg/g dry weight extract was obtained from extraction process of microalgae. Based on FTIR, and HPLC analysis, the microalgae carotenoid extracts contained β-carotene (C40H56) and lutein (C40H56O4). The IC50 value of microalgae carotenoid extract was 78.61 µg/mL. This study suggests that microalgae Mychonastes racemosus AUP1 are potential sources for obtaining carotenoid with strong antioxidant activity. In the future, the microalgae Mychonastes racemosus AUP1 has the potential for prospection of functional foods.

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Corrigendum to “Depsipeptides from a Guamanian Marine Cyanobacterium, Lyngbya bouillonii, with Selective Inhibition of Serine Proteases” [Tetrahedron Letters 51 (2010) 6718–6721]

Cited by 2 publications

References 1 publication

Dinghupeptins A–D, Chymotrypsin Inhibitory Cyclodepsipeptides Produced by a Soil-Derived Streptomyces

Dinghupeptins A–D, Chymotrypsin Inhibitory Cyclodepsipeptides Produced by a Soil-Derived Streptomyces

Carotenoid Profile of Freshwater Microalgae Mychonastes racemosus AUP1 and its Antioxidant properties

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