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
• Article Data: 1

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

General Description

MET-LYS-BRADYKININ is a bioactive peptide that is formed from the precursor protein kininogen. It is a member of the kinin family of peptides and plays a role in various physiological and pathological processes including inflammation, blood pressure regulation, and pain perception. MET-LYS-BRADYKININ is a potent vasodilator and has been implicated in the pathogenesis of conditions such as hypertension and rheumatoid arthritis. It exerts its effects by binding to bradykinin receptors and activating downstream signaling pathways. Research on MET-LYS-BRADYKININ continues to elucidate its role in health and disease, with potential implications for the development of new therapeutic approaches.

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.