SMTP-4
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| Category | Bioactive by-products |
| Catalog number | BBF-02468 |
| CAS | |
| Molecular Weight | 533.7 |
| Molecular Formula | C32H39NO6 |
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Description
SMTP-4 is a Staplabin homolog isolated from Stachybotrys microspora IFO30018. It enhanced the binding of Plasminogen to Fibrin.
Specification
| IUPAC Name | 2-[2-[(3E)-4,8-dimethylnona-3,7-dienyl]-3,5-dihydroxy-2-methyl-7-oxo-4,9-dihydro-3H-pyrano[2,3-e]isoindol-8-yl]-3-phenylpropanoic acid |
| Canonical SMILES | CC(=CCCC(=CCCC1(C(CC2=C(C=C3C(=C2O1)CN(C3=O)C(CC4=CC=CC=C4)C(=O)O)O)O)C)C)C |
| InChI | InChI=1S/C32H39NO6/c1-20(2)10-8-11-21(3)12-9-15-32(4)28(35)18-24-27(34)17-23-25(29(24)39-32)19-33(30(23)36)26(31(37)38)16-22-13-6-5-7-14-22/h5-7,10,12-14,17,26,28,34-35H,8-9,11,15-16,18-19H2,1-4H3,(H,37,38)/b21-12+ |
| InChI Key | HSOVHMPKFQKPSJ-CIAFOILYSA-N |
Reference Reading
1. Effect of Fermentation pH on Protein Bioaccessibility of Soymilk Curd with Added Tea Polyphenols As Assessed by in Vitro Gastrointestinal Digestion
Guangliang Xing, Xin Rui, Dan Wang, Mei Liu, Xiaohong Chen, Mingsheng Dong J Agric Food Chem. 2017 Dec 20;65(50):11125-11132. doi: 10.1021/acs.jafc.7b04456. Epub 2017 Dec 11.
The aim of this study was to compare the effect of fermentation pH on protein bioaccessibility of four soymilk curds enriched with tea polyphenols (TP). The curds were generated by fermentation with Weissella hellenica D1501 and the fermentation terminated at different pH values, namely at pH 5.7, 5.4, 5.1, and 4.8 (SMTP-5.7, SMTP-5.4, SMTP-5.1, SMTP-4.8). Particle-size distribution, soluble protein content, gel electrophoresis, and peptides content were monitored at oral, gastric, and intestinal levels. Results showed that SMTP-4.8 was the matrix most resistant to protein digestion in the gastric phase according to the soluble protein content. Similar particle size distribution and protein degradation patterns were observed for these curds in gastric and intestinal phase. However, there was a significant difference (P < 0.05) in the content of small peptides (<10 kDa) at the end of intestinal digestion among the four curds. Overall, terminating fermentation at pH 5.4-5.7 of soymilk curds enriched with TP is recommended.
2. Structure-activity relationships of 11 new congeners of the SMTP plasminogen modulator
Keiko Hasegawa, Haruki Koide, Weimin Hu, Naoko Nishimura, Ritsuko Narasaki, Yoshikazu Kitano, Keiji Hasumi J Antibiot (Tokyo). 2010 Oct;63(10):589-93. doi: 10.1038/ja.2010.101. Epub 2010 Sep 15.
The fungal metabolite Stachybotrys microspora triprenyl phenols (SMTPs) are small-molecule plasminogen modulators that enhance plasminogen activation. The SMTP molecule consists of a tricyclic γ-lactam moiety, an isoprene side-chain and an N-linked side-chain. Previous investigations have demonstrated that the N-linked side-chain is crucial for its activity. In this study, we have isolated 11 new SMTP congeners with a variety of N-linked side-chain structures, to investigate structure-activity relationships. Active compounds included congeners with a carboxyl or a sulfonic acid group in the N-linked side-chain, whereas not all the congeners with a carboxyl group were active. Of these congeners, that with methionine or tyrosine as the N-linked side-chain moiety was more active than that with an aliphatic amino acid. Congeners without ionizable group in the N-linked side-chain were essentially inactive.
3. SMTP-4D, -5D, -6D, -7D and -8D, a new series of the non-lysine-analog plasminogen modulators with a D-amino acid moiety
Weimin Hu, Yoshikazu Kitano, Keiji Hasumi J Antibiot (Tokyo). 2003 Oct;56(10):832-7. doi: 10.7164/antibiotics.56.832.
Staplabin and SMTPs, triprenyl phenol metabolites of the fungus Stachybotrys microspora, are a family of non-lysine-analog plasminogen modulators that enhance both activation and fibrin binding of plasminogen by modulating plasminogen conformation. These compounds, including SMTP-4, -5, -6, -7 and -8, have an amino acid or an amino alcohol moiety in their structure, and precursor amine feeding greatly increases the biosynthesis of a metabolite of interest. In the present study, we have isolated five novel SMTPs (designated SMTP-4D, -5D, -6D, -7D and -8D) from precursor D-amino acid-fed cultures. Physico-chemical properties as well as chromatographic behavior were distinct from those of the corresponding L-amino acid analogs, which are selectively accumulated in L-amino acid-fed cultures and share common properties with corresponding natural products. The D-series SMTPs enhanced urokinase-catalyzed plasminogen activation by 10-fold at 80 approximately 180 microM.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
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