26791-46-8

Basic information

• Product Name: H-ARG-ARG-ARG-ARG-OH
• Synonyms: H-ARG-ARG-ARG-ARG-OH
• CAS NO: 26791-46-8
• Molecular Formula: C24H50N16O5
• Molecular Weight: 642.76
• Mol File: 26791-46-8.mol

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-ARG-ARG-ARG-ARG-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-ARG-ARG-ARG-ARG-OH(26791-46-8)
• EPA Substance Registry System: H-ARG-ARG-ARG-ARG-OH(26791-46-8)

Safety Data

• Hazardous Substances Data: 26791-46-8(Hazardous Substances Data)

Usage

Uses

Used in Drug Delivery Systems:
Tetra-arginine is used as a carrier molecule in drug delivery systems for its ability to enhance the cellular uptake of therapeutic agents. Its positive charge allows for interactions with negatively charged drug molecules, facilitating their transport across cell membranes and improving the bioavailability and efficacy of the drugs.
Used in Gene Therapy:
In gene therapy, tetra-arginine serves as a vector for the delivery of genetic material into target cells. Its cell-penetrating properties enable the efficient transfer of nucleic acids, such as DNA or RNA, into cells, potentially leading to the correction of genetic defects or the silencing of disease-causing genes.
Used in Pharmaceutical Development:
Tetra-arginine is utilized in the development of novel pharmaceuticals, particularly those requiring targeted delivery to specific cell types or tissues. Its ability to penetrate cell membranes and transport molecules makes it a promising tool for the design of targeted therapeutic agents with enhanced specificity and reduced side effects.
Used in Cosmetics Industry:
Tetra-arginine is used as a penetration enhancer in cosmetics for improving the absorption of active ingredients into the skin. Its positive charge allows for better interaction with the negatively charged skin surface, facilitating the transport of beneficial compounds and enhancing their effectiveness.
Used in Food Industry:
In the food industry, tetra-arginine can be employed as a delivery agent for bioactive compounds, such as vitamins, antioxidants, or flavor enhancers. Its ability to cross biological barriers can improve the bioavailability and effectiveness of these compounds, leading to enhanced nutritional or sensory properties of food products.

Upstream product

• 56-86-0 L-glutamic acid 
• 74-79-3 L-arginine 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 

Relevant articles and documents

Effect of oligoarginine conjugation on the antiwrinkle activity and transdermal delivery of GHK peptide

GHK (Gly-His-Lys), a natural peptide found in human skin and plasma, has been widely used in the cosmeceutical and pharmaceutical fields. The hydrophilic GHK and GHK-Cu are limited in their abilities to penetrate deeply into skin; because of this, various strategies for their skin delivery have been developed. In this investigation, Arg4 was conjugated with GHK to get heptapeptide, GHK-R4, and then in vitro antiwrinkle activity and transdermal delivery were compared between GHK and GHK-R4. Notably, Arg4 conjugation accelerated the cellular penetration of GHK both in vitro and in vivo. Furthermore, higher in vitro antiwrinkle activity and collagen biosynthesis was obtained with GHK-R4 at much lower doses than with control R4-free GHK. The enhanced activity and delivery of GHK-R4 might be due to the cell penetrating ability and matrix metalloproteinase (MMP) inhibitory activity of R4 itself.

Modelling of prebiotic synthesis and selection of peptides under isothermal conditions and thermal cycling mode

The model peptide synthesis from mixtures of amino acids was carried out under the thermal cycling and isothermal modes. The compositions of the obtained mixtures of products and the primary amino acid sequence of the synthesized peptides were determined by Fourier transform ion cyclotron resonance mass spectrometry and tandem mass spectrometry in combination with high-performance liquid chromatography with the application of de novo sequencing of the synthesized products. The processes of abiogenous synthesis of peptides were shown to occur under relatively mild temperature conditions and give a substantially less number of peptides as compared with the possible statistical set. The evolution of the system takes place in the process of the synthesis in solid phase with the disappearance of a series of the most unstable peptides. The selection process with the formation of complementary peptides takes place in peptide synthesis under the thermal cyclic mode.