60254-82-2

Basic information

• Product Name: BETA-LIPOTROPIN, FRAGMENT 61-64
• Synonyms: tyrosyl-glycyl-glycyl-phenylalanyl;DES-MET5-METHIONINE ENKEPHALIN
• CAS NO: 60254-82-2
• Molecular Formula: C₂₂H₂₆N₄O₆
• Molecular Weight: 442.465
• Mol File: 60254-82-2.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 891°C at 760 mmHg
• Flash Point: 492.7°C
• Appearance: /
• Density: 1.339g/cm³
• Vapor Pressure: 4.37E-34mmHg at 25°C
• Refractive Index: 1.614
• PKA: 3.49±0.10(Predicted)
• CAS DataBase Reference: BETA-LIPOTROPIN, FRAGMENT 61-64(CAS DataBase Reference)
• NIST Chemistry Reference: BETA-LIPOTROPIN, FRAGMENT 61-64(60254-82-2)
• EPA Substance Registry System: BETA-LIPOTROPIN, FRAGMENT 61-64(60254-82-2)

Safety Data

• Hazardous Substances Data: 60254-82-2(Hazardous Substances Data)

Usage

General Description

BETA-LIPOTROPIN, FRAGMENT 61-64 is a chemical fragment derived from the protein beta-lipotropin. It is a peptide composed of the amino acid sequence 61-64 of beta-lipotropin. This fragment is believed to have potential effects on the regulation of appetite and metabolism, as well as potential roles in pain modulation and stress response. Studies have shown that this peptide may have some neuroprotective and anti-inflammatory properties, and it has been investigated for its potential therapeutic applications in conditions such as obesity, chronic pain, and neurodegenerative diseases. However, further research is needed to fully understand the mechanisms and potential benefits of BETA-LIPOTROPIN, FRAGMENT 61-64.

InChI:InChI=1/C22H26N4O6/c23-17(10-15-6-8-16(27)9-7-15)21(30)25-12-19(28)24-13-20(29)26-18(22(31)32)11-14-4-2-1-3-5-14/h1-9,17-18,27H,10-13,23H2,(H,24,28)(H,25,30)(H,26,29)(H,31,32)/t17-,18-/m0/s1

Upstream product

• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 112883-29-1 N-Fmoc-Tyr-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 60117-24-0 H-Tyr-Gly-Gly-Phe-Leu-NH₂ 
• 58822-25-6 Leu-enkephalin 
• 77739-20-9 alpha-Neoendorphin (Porcine) 

Relevant articles and documents

A Facile Synthesis of NODASA-Functionalized Peptide

Herein, we report a mild and efficient synthesis of a NODASA-functionalized peptide, which was initiated with a Michael addition reaction between monomethyl fumarate and 1,4,7-triazacyclononane.

SPECIFICITY AND MOLECULAR PROPERTIES OF PENICILLOLYSIN, A METALLOPROTEINASE FROM PENICILLUM CITRINUM

The specificity and mode of action of penicillolysin, a metalloproteinase from Penicillum citrinum, were investigated with several bioactive-oligopeptides.The enzyme showed a high affinity toward the Pro-X (X = Gln, Lys, Leu or Arg) bonds of substance P, dynorphin A (1-13), neurotensin and chicken brain pentapeptide, and the R-R bonds in dynorphin A and neurotensin.Preferential cleavages of bonds by the enzyme with hydrophobic amino acid residues at the P1 position were observed on the peptides used.The specificity of penicillolysin differs from that of other metallopropteinases.The Mr and pI were determined as 18000 and 9.6, respectively.The first 50 amino acids in the N-terminal region were TKETCSNASRKSALEKALSNTVKLANAAATAARSGSASKFSEYEKTTSSS.CD spectra on the hollo- and apo-enzymes of penicillolysin were studied.