67869-62-9

Basic information

• Product Name: GLY-PRO-ARG-PRO
• Synonyms: FIBRINOLYSIS INHIBITNG FACTOR;glycine-proline-arginine-proline;M.W. 425.49 C18H31N7O5;GI-GPx;GPX2;GSHPX-GI;Fibrinolysis Inhibitng Factor| H-Gly-Pro-Arg-Pro-OH;glycyl-prolyl-arginyl-proline
• CAS NO: 67869-62-9
• Molecular Formula: C18H31N7O5
• Molecular Weight: 425.48
• Product Categories: Peptide;Blood;Clotting FactorsPeptides for Cell Biology;Clotting InhibitorsProteins and Derivatives;Coagulation Proteins and Reagents;Extracellular Matrix Peptides (ECM);Immune Cell Signaling and Blood;Plasma&Blood Proteins;Fibrinogen/Thrombin
• Mol File: 67869-62-9.mol
• Article Data: 6

Chemical Properties

• Melting Point: 123-125 °C
• Appearance: white to off-white powder
• Density: 1.55 g/cm³
• Refractive Index: 1.691
• Storage Temp.: −20°C
• PKA: 3.41±0.20(Predicted)
• CAS DataBase Reference: GLY-PRO-ARG-PRO(CAS DataBase Reference)
• NIST Chemistry Reference: GLY-PRO-ARG-PRO(67869-62-9)
• EPA Substance Registry System: GLY-PRO-ARG-PRO(67869-62-9)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 67869-62-9(Hazardous Substances Data)

Usage

Uses

Gly-Pro-Arg-Pro (GPRP) has been used for the formation of crystal composed of GPRP and the 30kDa C-terminal fragment from the γ chain of fibrinogen (rFbgγC30), cloned and expressed in Pichia pastoris.

General Description

Gly-Pro-Arg-Pro is a peptide that mimics the N-terminal Gly-Pro-Arg region in the α chain of fibrin protein.

Biochem/physiol Actions

Product does not compete with ATP.

InChI:InChI=1/C18H31N7O5/c19-10-14(26)24-8-2-5-12(24)15(27)23-11(4-1-7-22-18(20)21)16(28)25-9-3-6-13(25)17(29)30/h11-13H,1-10,19H2,(H,23,27)(H,29,30)(H4,20,21,22)

Upstream product

• 41324-66-7 H-Pro-OBzl 
• 148205-61-2 Z(OMe)-Arg(NO₂)-Pro-OBzl 
• 23828-53-7 Z-Gly-Pro-NHNH₂ 
• 57294-41-4 Z-Gly-Pro-OBzl 
• 23234-71-1 Z(OMe)-Arg(NO₂)-OH 
• 85918-68-9 H-Arg(NO₂)-Pro-OBzl 
• 776334-65-7 Boc-Gly-Pro-Arg(NO₂)-Pro-OBzl 
• 134303-57-4 Boc-Pro-Arg(NO₂)-Pro-OBzl 
• 54046-53-6 Boc-Arg(NO₂)-Pro-OBzl 
• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 
• 2188-18-3 Boc-Arg(NO₂)-OH 
• 107994-61-6 Boc-Gly-Pro-Arg-Pro-OMe 
• 785737-07-7 C₂₂H₃₈N₆O₆ 
• 60397-21-9 N^α-tert-Butyloxycarbonyl-prolyl-arginine 

Relevant articles and documents

Sustainable Peptide Synthesis Enabled by a Transient Protecting Group

The growing interest in synthetic peptides has prompted the development of viable methods for their sustainable production. Currently, large amounts of toxic solvents are required for peptide assembly from protected building blocks, and switching to water as a reaction medium remains a major hurdle in peptide chemistry. We report an aqueous solid-phase peptide synthesis strategy that is based on a water-compatible 2,7-disulfo-9-fluorenylmethoxycarbonyl (Smoc) protecting group. This approach enables peptide assembly under aqueous conditions, real-time monitoring of building block coupling, and efficient postsynthetic purification. The procedure for the synthesis of all natural and several non-natural Smoc-protected amino acids is described, as well as the assembly of 22 peptide sequences and the fundamental issues of SPPS, including the protecting group strategy, coupling and cleavage efficiency, stability under aqueous conditions, and crucial side reactions.

Selective antifungal activity of shorter active analogues of Bactenecin7 against Fusarium moniliforme

Bactenecin7 (Bac7), a cationic antibacterial peptide, contains a repeating region of Xaa-Pro-Arg-Pro (Xaa = hydrophobic residue). To investigate the structure and property of a Pro/Arg-rich region, we synthesized a series of peptides, Xaa-Pro-Arg-Pro (Xaa

Amino acids and peptides. XVI. Synthesis of N-terminal tetrapeptide analogs of fibrin α-chain and their inhibitory effects on fibrinogen/thrombin clotting

N-Terminal tetrapeptide analogs of fibrin α-chain were synthesized by the solution method using a new active ester, the ester of the oxime of p-nitroacetophenone, and by the solid-phase method. Their inhibitory effects on fibrinogen/thrombin clotting were examined. Of the synthetic peptides, amide analogs of Gly-Pro-Arg-Pro exhibited a more potent inhibitory effect.