13054-03-0

Usage

Uses

Used in Pharmaceutical and Medical Research:
GLY-PRO-GLY-GLY is used as a potential therapeutic agent for its biological activities, such as promoting collagen synthesis or acting as a substrate for enzymes involved in protein degradation.
Used in Collagen Synthesis:
In the pharmaceutical industry, GLY-PRO-GLY-GLY is used as a promoter of collagen synthesis, which is essential for maintaining skin elasticity, wound healing, and tissue repair.
Used in Protein Degradation:
GLY-PRO-GLY-GLY is used as a substrate for enzymes involved in protein degradation, which can be beneficial in the development of treatments for various diseases and conditions related to protein misfolding or aggregation.
Used in Structural Proteins:
In the biotechnology industry, GLY-PRO-GLY-GLY is used in the design and development of structural proteins, where its role in protein folding and stability can be leveraged to create more effective and stable therapeutic proteins.

InChI:InChI=1/C11H18N4O5/c12-4-9(17)15-3-1-2-7(15)11(20)14-5-8(16)13-6-10(18)19/h7H,1-6,12H2,(H,13,16)(H,14,20)(H,18,19)

Upstream product

• 264226-81-5 t-BuOCO-Gly-L-Pro-Gly-Gly-OH 
• 41324-66-7 H-Pro-OBzl 
• 2644-64-6 1,2-dipalmitoyl-rac-glycero-3-phosphatidylcholine 
• 14296-92-5 (S)-1-(2-(tert-butoxycarbonylamino)acetyl)pyrrolidine-2-carboxylic acid 
• 29776-78-1 (S)-1-(2-tert-butoxycarbonylaminoacetyl)pyrrolidine-2-carboxylic acid benzyl ester 

Relevant academic research and scientific papers

Peptidophospholipids: Synthesis, phospholipase A2 catalyzed hydrolysis, and application to development of phospholipid prodrugs

New phospholipid analogues incorporating sn-2-peptide substituents have been prepared to probe the fundamental structural requirements for phospholipase A2 catalyzed hydrolysis of PLA2-directed synthetic substrates. Two structurally

The L-Proline Residue as a 'Break-point' in Metal - Peptide Systems

Results are reported of a potentiometric and spectrophotometric study of the H+ and Cu2+ complexes of the tetrapeptides X-Gly-Gly-Gly, Gly-X-Gly-Gly, Gly-Gly-X-Gly, and Gly-Gly-Gly-X where X is the proline (Pro) and sarcosine (Sar) residue (Gly=glycine).All the tetrapeptides (HL) form the series of complexes , -1L>, -2L>, and -3L> (charges omitted).The ligands Gly-X-Gly-Gly also form the bis-complex, .When inserted in a peptide chain the Pro and Sar residues cannot co-ordinate to Cu2+ through their peptide nitrogens since they do not possess ionizable protons.In addition the Pro residue tends to force the peptide chain to form a 'β-turn' and so adopt a 'bent' conformation.These studies demonstrate the formation of a large chelate ring when tetrapeptides containing Pro (and , to a smaller extent, Sar) in the second or third positions co-ordinate to Cu2+.This ring spans the terminal residues of the peptide chain and locks the peptide into a 'bent' or 'horse-shoe' shaped conformation.Cu2+ could therefore play an important role in activating oligopeptides (e.g. neuropeptides) containing proline.