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Neo-kyotorphin is a peptide compound derived from kyotorphin, a naturally occurring brain peptide known for its pain-relieving properties. First discovered in 2014, it has been found to possess a more potent analgesic effect than kyotorphin, likely due to its unique chemical structure that facilitates easier passage through the blood-brain barrier. As a synthetic peptide, neo-kyotorphin is composed of two amino acids and has a molecular formula of C17H24N4O4.

83759-54-0

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83759-54-0 Usage

Uses

Used in Pharmaceutical Industry:
Neo-kyotorphin is used as a potential analgesic agent for the treatment of chronic pain conditions. Its stronger pain-relieving effects compared to kyotorphin make it a promising candidate for pharmaceutical development.
Used in Medical Research:
Neo-kyotorphin is used as a subject of study in medical research to further understand its analgesic properties and explore its potential applications in pain management. This research may lead to the development of new therapeutic strategies for various chronic pain conditions.
Used in Drug Delivery Systems:
Neo-kyotorphin is used as a component in drug delivery systems designed to improve the efficacy and bioavailability of analgesic treatments. By incorporating neo-kyotorphin into these systems, researchers aim to enhance the delivery of pain-relieving medications to the target areas in the body, potentially leading to more effective pain management.

Check Digit Verification of cas no

The CAS Registry Mumber 83759-54-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,3,7,5 and 9 respectively; the second part has 2 digits, 5 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 83759-54:
(7*8)+(6*3)+(5*7)+(4*5)+(3*9)+(2*5)+(1*4)=170
170 % 10 = 0
So 83759-54-0 is a valid CAS Registry Number.
InChI:InChI=1/C28H47N9O9/c1-15(39)22(30)26(44)37-21(14-38)25(43)34-18(5-2-3-11-29)23(41)36-20(13-16-7-9-17(40)10-8-16)24(42)35-19(27(45)46)6-4-12-33-28(31)32/h7-10,15,18-22,38-40H,2-6,11-14,29-30H2,1H3,(H,34,43)(H,35,42)(H,36,41)(H,37,44)(H,45,46)(H4,31,32,33)/t15-,18+,19+,20+,21+,22+/m1/s1

83759-54-0SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name L-Threonyl-L-seryl-L-lysyl-L-tyrosyl-N<sup>5</sup>-(diaminomethylene)-L-ornithine

1.2 Other means of identification

Product number -
Other names taiwanin E methyl ether

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:83759-54-0 SDS

83759-54-0Downstream Products

83759-54-0Relevant academic research and scientific papers

Diffusion based kinetic selectivity modulation of enzymatic proteolysis in a microfluidic reactor: Experimental analysis and stochastic modeling

Elagli, Adil,Laurette, Simon,Treizebre, Anthony,Bocquet, Bertrand,Froidevaux, Renato

, p. 3873 - 3882 (2014/01/06)

Microreactors enable new experimental ways for enzyme engineering. In this context, we show that the liquid-liquid parallel laminar flows in microchannels cause a kinetic selectivity modification of proteolytic enzymatic reaction involving hemoglobin and pepsin, reaction that generates numerous bioactive peptides at different advancement state. Here we show that this diffusion based kinetic modulation induces an altered peptides appearance kinetics for a part of the initial substrate population. Indeed, microfluidic and conventional batch experiments performed in the same reaction conditions lead to strong differences in the resulting peptidic profiles obtained by reversed-phase high-performance liquid chromatography. Such differences are explained by the laminar flow diffusive conditions inside microchannels and are supported by a stochastic algorithm based on the Michaelis-Menten equation. Several bioactive peptides are identified by mass spectrometry and show the potential of such methodology in peptides screening from a complex proteolysis but also for selective peptides preparation by microfluidics.

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