67869-62-9

Usage

Uses

Used in Pharmaceutical Industry:
GLY-PRO-ARG-PRO is used as a component in the formation of crystals for potential therapeutic applications. The expression is: GLY-PRO-ARG-PRO is used as a component in the formation of crystals composed of GPRP and the 30kDa C-terminal fragment from the γ chain of fibrinogen (rFbgγC30), cloned and expressed in Pichia pastoris. This may have potential uses in the development of new drugs or therapies.

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

• 134303-72-3 Z-Gly-Pro-Arg(NO₂)-Pro-OBzl 
• 54046-53-6 Boc-Arg(NO₂)-Pro-OBzl 
• 41324-66-7 H-Pro-OBzl 
• 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 
• 2188-18-3 Boc-Arg(NO₂)-OH 
• 83674-60-6 (S)-1-((S)-2-{[(S)-1-(2-tert-Butoxycarbonylamino-acetyl)-pyrrolidine-2-carbonyl]-amino}-5-guanidino-pentanoyl)-pyrrolidine-2-carboxylic acid 
• 148205-61-2 Z(OMe)-Arg(NO₂)-Pro-OBzl 
• 23234-71-1 Z(OMe)-Arg(NO₂)-OH 
• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 
• 23828-53-7 Z-Gly-Pro-NHNH₂ 
• 57294-41-4 Z-Gly-Pro-OBzl 
• 74-79-3 L-arginine 

Relevant academic research and scientific papers

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.

Synthesis of modified fragments of fibrinogen and their effect on the activity of proteolytic enzymes

New analogues of the Gly-Pro-Arg and Arg-Gly-Asp fragments of fibrinogen were synthesized: Gly-Pro-Arg-Pro (I), Gly-Pro-Arg-Pro-Met-OMe (II), Gly-Pro-Arg-Pro-Phe (III), Gly-Pro-Arg-Pro-Asp (IV), Gly-Pro-Arg-Pro-Glu (V), and Arg-Asn-Trp-Asp (VI). Their eff

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

Method and composition for treating IgE-mediated allergies

The present invention relates to a method and preparations for reducing IgE antibodies to allergens in allergic subjects wherein substance P and an allergen or fragments of allergens or haptens acting as allergens are administered together to the allergic subjects. The method can be used to treat humans and animals including dogs, cats, horses and subhuman primates.

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.

Novel substrate peptides

A peptide substrate for myristoylating enzymes is disclosed having an amino acid sequence selected from the group consisting of the following sequences or a physiologically acceptable amide or salt derivative thereof: STR1 wherein R=Ala, Asn, Gln or Ser; S=Ala, Arg, Gln, Glu, Phe or Ser; T=Ala or Lys; W=Ala or Ser; X=Ala, Tyr, or Lys; Y=Arg or Pro; and Z=Arg, Leu or Lys.