Gln-Gln

Gln-Gln pairs two glutamine residues offering strong hydrogen-bonding potential and conformational adaptability. Researchers analyze its behavior across pH conditions to study amide-mediated interactions. The dipeptide serves as a model for polar side-chain contributions. Applications include folding studies, enzymatic recognition research, and peptide assembly design.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Gln-Gln(CAS 54419-93-1)

CAT No: R2351

CAS No:54419-93-1

Synonyms/Alias:H-Gln-Gln-OH;Gln-Gln;54419-93-1;L-GLUTAMINYL-L-GLUTAMINE;glutaminylglutamine;Glutaminyl-Glutamine;QQ dipeptide;Q-Q Dipeptide;CHEBI:73846;Glutamine Glutamine dipeptide;Glutamine-Glutamine dipeptide;CHEMBL438960;(2S)-5-amino-2-[[(2S)-2,5-diamino-5-oxopentanoyl]amino]-5-oxopentanoic acid;(S)-5-Amino-2-((S)-2,5-diamino-5-oxopentanamido)-5-oxopentanoic acid;MFCD00038689;L-Gln-L-Gln;N2-Glutaminylglutamine;H-L-Gln-L-Gln-OH;SCHEMBL19375;N2-L-Glutaminyl-L-glutamine;DTXSID001313028;QQ;BDBM50188528;Q27144168;

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M.F/Formula
C10H18N4O5
M.W/Mr.
274.27
Sequence
One Letter Code:QQ
Three Letter Code:H-Gln-Gln-OH

Gln-Gln, also known as L-Glutaminyl-L-Glutamine or glutamine dipeptide, is a synthetic dipeptide composed of two glutamine residues linked via a peptide bond. This compound is widely recognized for its stability and solubility compared to free glutamine, making it an attractive molecule for various research and biotechnological applications. The unique dipeptide structure of Gln-Gln confers enhanced resistance to hydrolysis and degradation in aqueous environments, allowing for more controlled and efficient delivery of glutamine in experimental systems. Because of these properties, it serves as a valuable tool in studies requiring sustained glutamine availability, particularly in cell culture and metabolic research where glutamine is a critical nutrient. Its compatibility with a range of experimental setups and its ability to act as a stable glutamine reservoir underscore its importance in scientific investigations.

Cell Culture Supplementation: In cell biology and tissue engineering, Gln-Gln finds extensive use as a glutamine source in culture media. Researchers often prefer this dipeptide over free glutamine due to its increased stability, which minimizes the accumulation of toxic byproducts such as ammonia that can result from glutamine breakdown. By providing a more consistent and prolonged supply of glutamine, Gln-Gln supports optimal cell growth, viability, and productivity in both adherent and suspension cell lines. This is particularly relevant in the cultivation of hybridoma, CHO, and other mammalian cells commonly used in the production of recombinant proteins and monoclonal antibodies.

Metabolic Studies: Glutaminyl-glutamine dipeptide is frequently employed in metabolic flux analyses and nutrient tracing experiments. Its resistance to rapid degradation allows for precise control over glutamine concentrations in experimental systems, facilitating the investigation of glutamine metabolism, uptake, and utilization in various cell types. By using isotopically labeled forms of Gln-Gln, researchers can track metabolic pathways and elucidate the roles of glutamine in biosynthetic processes, energy production, and cellular signaling. This application is particularly valuable in cancer metabolism research, where altered glutamine utilization is a hallmark of many tumor cells.

Bioprocess Optimization: In the field of bioprocessing and industrial biotechnology, Gln-Gln is incorporated into fed-batch and perfusion cultures to enhance productivity and product quality. Its stability ensures a steady release of glutamine, reducing the risk of nutrient depletion and toxic byproduct formation over extended culture periods. This contributes to improved yields of biologics such as therapeutic proteins, enzymes, and vaccines, while supporting cell health and longevity. Process engineers often leverage the benefits of the dipeptide format to fine-tune nutrient delivery strategies and maximize process efficiency.

Nutritional Biochemistry Research: The dipeptide is also utilized in studies exploring amino acid transport, absorption, and metabolism in various biological systems. Gln-Gln serves as a model compound to investigate peptide transporter activity, intestinal uptake mechanisms, and the comparative bioavailability of dipeptide versus free amino acid forms. Such research provides insights into nutrient assimilation and the physiological relevance of peptide-based nutrient delivery, informing the development of advanced nutritional supplements and functional foods.

Protein Engineering and Structural Biology: In structural and functional studies of peptides and proteins, Gln-Gln can be used as a model substrate or as a building block for the synthesis of larger peptides. Its defined structure and predictable behavior make it suitable for investigating peptide bond formation, enzymatic hydrolysis, and the influence of sequence context on peptide stability. Researchers may also employ it in crystallization trials, NMR studies, or enzymatic assays to probe protein-peptide interactions and enzyme specificity, contributing to a deeper understanding of protein chemistry.

Peptide Drug Development: Within the realm of peptide-based drug discovery, Gln-Gln offers a valuable scaffold for the design and optimization of therapeutic peptides. Its physicochemical properties and metabolic stability can be leveraged to enhance peptide pharmacokinetics and bioavailability in preclinical studies. Medicinal chemists may use it as a template for the synthesis of novel peptide analogues, peptidomimetics, or delivery vehicles, further expanding the toolkit for innovative drug development and delivery strategies.

InChI
InChI=1S/C10H18N4O5/c11-5(1-3-7(12)15)9(17)14-6(10(18)19)2-4-8(13)16/h5-6H,1-4,11H2,(H2,12,15)(H2,13,16)(H,14,17)(H,18,19)/t5-,6-/m0/s1
InChI Key
LOJYQMFIIJVETK-WDSKDSINSA-N

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