550-19-6

Basic information

• Product Name: MET-LYS-BRADYKININ
• Synonyms: H-MET-LYS-ARG-PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG-OH;MET-LYS-BRADYKININ;[MET-LYS0] BRADYKININ;MET-LYS-ARG-PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG;MET-LYS-ARG-PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG 3ACOH 2H2O;METHIONYL-LYSYL-BRADYKININ (HUMAN, BOVINE);METHIONYL-LYSYL-BRADYKININ (HUMAN, BOVINE) 3ACOH 2H2O;met-lys-bradykini
• CAS NO: 550-19-6
• Molecular Formula: C₆₁H₉₄N₁₈O₁₃S
• Molecular Weight: 1319.58
• Mol File: 550-19-6.mol

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 1.46g/cm³
• Refractive Index: 1.681
• Storage Temp.: -15°C
• PKA: 3.34±0.10(Predicted)
• CAS DataBase Reference: MET-LYS-BRADYKININ(CAS DataBase Reference)
• NIST Chemistry Reference: MET-LYS-BRADYKININ(550-19-6)
• EPA Substance Registry System: MET-LYS-BRADYKININ(550-19-6)

Safety Data

• Hazardous Substances Data: 550-19-6(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
MET-LYS-BRADYKININ is used as a therapeutic agent for its vasodilatory properties, which can help in managing conditions related to blood pressure regulation, such as hypertension.
Used in Inflammation Management:
In the pharmaceutical industry, MET-LYS-BRADYKININ is utilized as an anti-inflammatory agent, particularly for conditions like rheumatoid arthritis, where its role in modulating inflammatory responses can be beneficial.
Used in Pain Management:
MET-LYS-BRADYKININ is employed as an analgesic agent, targeting pain perception pathways and providing relief in various pain-related conditions.
Used in Research Applications:
In the research field, MET-LYS-BRADYKININ serves as a valuable tool for studying the molecular mechanisms underlying inflammation, blood pressure regulation, and pain perception, contributing to the development of novel therapeutic strategies.

InChI:InChI=1/C61H94N18O13S/c1-93-32-25-39(63)50(82)72-40(19-8-9-26-62)51(83)73-41(20-10-27-68-60(64)65)56(88)79-31-14-24-48(79)58(90)78-30-12-22-46(78)54(86)70-35-49(81)71-43(33-37-15-4-2-5-16-37)52(84)76-45(36-80)57(89)77-29-13-23-47(77)55(87)75-44(34-38-17-6-3-7-18-38)53(85)74-42(59(91)92)21-11-28-69-61(66)67/h2-7,15-18,39-48,80H,8-14,19-36,62-63H2,1H3,(H,70,86)(H,71,81)(H,72,82)(H,73,83)(H,74,85)(H,75,87)(H,76,84)(H,91,92)(H4,64,65,68)(H4,66,67,69)/t39-,40-,41-,42-,43-,44-,45-,46-,47-,48-/m0/s1

Relevant articles and documents

Substrate specificity studies of the cysteine peptidases falcipain-2 and falcipain-3 from Plasmodium falciparum and demonstration of their kininogenase activity

We studied the substrate specificity requirements of recombinant cysteine peptidases from Plasmodium falciparum, falcipain-2 (FP-2) and falcipain-3 (FP-3), using fluorescence resonance energy transfer (FRET) peptides as substrates. Systematic modifications were introduced in the lead sequence Abz-KLRSSKQ-EDDnp (Abz = ortho-aminobenzoic acid; EDDnp = N-[2,4-dinitrophenyl] ethylenediamine) resulting in five series assayed to map S3-S ′2 subsite specificity. Despite high sequence identity and structural similarity between FP-2 and FP-3, noteworthy differences in substrate specificity were observed. The S1 subsite of FP-2 preferentially accommodates peptides containing the positively charged residue Arg in P 1, while FP-3 has a clear preference for the hydrophobic residue Leu in this position. The S2 subsite of FP-2 and FP-3 presents a strict specificity for hydrophobic residues, with Leu being the residue preferred by both enzymes. FP-2 did not show preference for the residues present at P 3, while FP-3 hydrolysed the peptide Abz-ALRSSRQ-EDDnp, containing Ala at P3, with the highest catalytic efficiency of all series studied. FP-2 has high susceptibility for substrates containing hydrophobic residues in P′1, while FP-3 accommodates well peptides containing Arg in this position. The S′2 subsite of both enzymes demonstrated broad specificity. In addition, radioimmunoassay experiments indicated that kinins can be generated by FP-2 and FP-3 proteolysis of high molecular weight kininogen (HK). Both enzymes excised Met-Lys-bradykinin, Lys-bradykinin and bradykinin from the fluorogenic peptide Abz-MISLMKRPPGFSPFRSSRI-NH2, which corresponds to the Met 375 to Ile393 sequence of HK. The capability of FP-2 and FP-3 to release kinins suggests the involvement of these enzymes in the modulation of malaria pathophysiology.