164991-89-3 Usage
Description
Segetalin B is a cyclopentapeptide derived from the seeds of Vaccaria segetalis (Caryophyllaceae), characterized by its needle-like appearance and a melting point of 153-155°C. It exhibits estrogen-like activity, making it a potential candidate for pharmaceutical applications.
Uses
Used in Pharmaceutical Industry:
Segetalin B is used as a pharmaceutical agent for its estrogen-like activity, which can be beneficial in treating conditions related to hormonal imbalances or deficiencies.
Used in Drug Delivery Systems:
Similar to gallotannin, segetalin B can be incorporated into drug delivery systems to enhance its therapeutic efficacy and bioavailability. This may involve the use of organic or metallic nanoparticles as carriers for targeted delivery to specific tissues or cells.
Pharmacology
Examples of naturally occurring bioactive cyclopeptides are Segetalins A and B，which were isolated from Vaccaria segetalis (Caryophyllacea) and
were shown to have estrogen-like activity. The seeds of Vaccaria segetalis are used in Chinese folk medicine to activate blood flow, to promote milk secretion, and to
treat amenorrhea and breast infections.
That Segetalin A and Segetalin B have the Try-Ala-Gly-Val (WAGV) sequence in
common indicates this is the biologically active part of the molecules. NMR
studies indicate,however,that the orientation of the Val residue is different in the
molecules.The effect of this amino acid on the activity of the compounds might
not be very important.
Check Digit Verification of cas no
The CAS Registry Mumber 164991-89-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,6,4,9,9 and 1 respectively; the second part has 2 digits, 8 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 164991-89:
(8*1)+(7*6)+(6*4)+(5*9)+(4*9)+(3*1)+(2*8)+(1*9)=183
183 % 10 = 3
So 164991-89-3 is a valid CAS Registry Number.
164991-89-3Relevant articles and documents
Characterization of the Fast and Promiscuous Macrocyclase from Plant PCY1 Enables the Use of Simple Substrates
Ludewig, Hannes,Czekster, Clarissa M.,Oueis, Emilia,Munday, Elizabeth S.,Arshad, Mohammed,Synowsky, Silvia A.,Bent, Andrew F.,Naismith, James H.
, p. 801 - 811 (2018)
Cyclic ribosomally derived peptides possess diverse bioactivities and are currently of major interest in drug development. However, it can be chemically challenging to synthesize these molecules, hindering the diversification and testing of cyclic peptide leads. Enzymes used in vitro offer a solution to this; however peptide macrocyclization remains the bottleneck. PCY1, involved in the biosynthesis of plant orbitides, belongs to the class of prolyl oligopeptidases and natively displays substrate promiscuity. PCY1 is a promising candidate for in vitro utilization, but its substrates require an 11 to 16 residue C-terminal recognition tail. We have characterized PCY1 both kinetically and structurally with multiple substrate complexes revealing the molecular basis of recognition and catalysis. Using these insights, we have identified a three residue C-terminal extension that replaces the natural recognition tail permitting PCY1 to operate on synthetic substrates. We demonstrate that PCY1 can macrocyclize a variety of substrates with this short tail, including unnatural amino acids and nonamino acids, highlighting PCY1's potential in biocatalysis.
