53-73-6

Usage

Uses

Used in Pharmaceutical Industry:
ASN-ARG-VAL-TYR-VAL-HIS-PRO-PHE is used as a pressor agent for the treatment of various hypotensive states. It is particularly useful in controlling acute hypotension during the administration of general anesthetics that sensitize the heart to the effects of catecholamines. The pressor effect of this polypeptide is due to an increase in peripheral resistance, as it constricts resistance vessels with little or no stimulating action on the heart and minimal effect on the capacitance vessels.
Additionally, it is available as a lyophilized powder for injection, with dosages ranging from 0.5–2.5 mg diluted in 500 mL of sodium chloride injection or 5% dextrose for injection, to be administered by continuous infusion.

Originator

Hypertensin,Ciba,W. Germany,1961

Manufacturing Process

48 mg (0.042 mmol) of L-asparaginyl-L-arginyl-L-valyl-L-tyrosyl-L-valyl-Lhistidyl- L-prolyl-L-phenylalanine methyl ester trihydrochloride are suspended in 0.5 ml of methanol, and treated gradually in the course of one hour with 0.3 ml of N-caustic soda solution (about 7 equivalents) so that the pH value of the solution is maintained between 10.5 and 11.5. After a further 30 minutes the solution is freed from methanol under vacuum at room temperature, adjusted with 1 N acetic acid to pH 7.4 and lyophilized. The residual mixture of free peptide and inorganic salts (79 mg) is fractionated by countercurrent distribution in the system butanol/0.1 N ammonium hydroxide. The pure octapeptide is obtained as a colorless powder which is soluble in water and methanol, more sparingly soluble in ethanol, and insoluble in acetone.

InChI:InChI=1/C49H70N14O11/c1-26(2)39(61-42(67)33(12-8-18-55-49(52)53)57-41(66)32(50)23-38(51)65)45(70)58-34(20-29-14-16-31(64)17-15-29)43(68)62-40(27(3)4)46(71)59-35(22-30-24-54-25-56-30)47(72)63-19-9-13-37(63)44(69)60-36(48(73)74)21-28-10-6-5-7-11-28/h5-7,10-11,14-17,24-27,32-37,39-40,64H,8-9,12-13,18-23,50H2,1-4H3,(H2,51,65)(H,54,56)(H,57,66)(H,58,70)(H,59,71)(H,60,69)(H,61,67)(H,62,68)(H,73,74)(H4,52,53,55)/t32-,33-,34-,35-,36-,37-,39-,40-/m0/s1

Upstream product

• 68858-20-8 Fmoc-Val-OH 
• 71989-31-6 Fmoc-Pro-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 132388-59-1 L-Asn(Trt) 
• 109425-51-6 Fmoc-His(Trt)-OH 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 

Downstream Products

• 58059-29-3 6-(p-chlorophenyl)-3-chloropyridazine 

Relevant academic research and scientific papers

Interfacing droplet microfluidics with matrix-assisted laser desorption/ionization mass spectrometry: Label-free content analysis of single droplets

Droplet-based microfluidic systems have become a very powerful tool to miniaturize chemical and biological reactions. However, droplet content analysis remains challenging and relies almost exclusively on optical methods such as fluorescence spectroscopy. Hence, labeling of the analyte is typically required which impedes a more universal applicability of microdroplets. Here we present a novel interface coupling droplet microfluidics and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry for label-free content analysis of single droplets. Nanoliter aqueous droplets immersed in perfluorinated oil are created in a microfluidic T-junction, transferred into a capillary, and deposited on a high-density microarray MALDI plate mounted on a motorized xy-stage. The fully automated system is robust and reliable due to two unique features. First, a simple optical droplet detection system is used to synchronize stage movement and exit of droplets from the capillary. Second, the microarray plate contains an array of over 26 000 hydrophilic spots within a hydrophobic coating, each spot acting as a recipient to confine the droplets and to prevent cross-contamination. The MALDI matrix can also be applied using our system by spotting matrix droplets on the microarray in a separate run. To demonstrate the potential of our system, we studied the enzymatic cleavage of angiotensin I by angiotensin converting enzyme and monitored the increasing concentration of the product angiotensin II over time. The interface provides a robust and fully automated method for rapid label-free and information-rich content analysis of single droplets. With the high number of droplets per plate, this method is particularly suitable for high-throughput screening applications.

IMPROVEMENTS IN SOLID PHASE PEPTIDE SYNTHESIS

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

INHIBITORY OCTAPEPTIDES ANGIOTENSIN II

Octapeptide derivatives characterized by an oxygen or sulfur-containing moiety in the C-terminal position are potent inhibitors of the pharmacological effects of Angiotensin and possess the additional advantage of a favorable antagonist/agonist ratio.