Taiy Chemical
Cyclo(-D-Phe-GWAVGHLL)
Synonym Cyclo(-D-Phe-GWAVGHLL)
Species Human
Protein Accession NA
Purity ≥ 95%
Endotoxin Level <1.0 EU per 1 μg of the protein
Biological Activity NA
Expression System E. coli
Fusion Tag NA
Predicted Molecular Mass 1183.3 Da
Formulation Lyophilized from a 0.2 μm filtered solution in 30% acetonitrile and 0.1% trifluoroacetic acid
Reconstitution It is recommended to reconstitute the lyophilized product in sterile water at a concentration of 100 μg/ml
Storage & Stability Store at -20°C upon receipt, stable for up to 3 months at -20°C. For long term storage, store at -80°C.
FAQ

Can you explain what Cyclo(D-Phe-GWAVGHLL) is and its primary benefits?

Cyclo(D-Phe-GWAVGHLL) is an innovative and specialized cyclopeptide compound known for its unique properties and potential applications in various fields, especially in health and wellness. This compound consists of a sequence of amino acids that are arranged in a cyclic format, which can often confer specific stability and biochemical properties not found in linear peptides. The incorporation of the D-phenylalanine (D-Phe) further enhances these characteristics, potentially offering increased resistance to enzymatic degradation and a higher degree of specificity in interactions with biological systems. The benefits of Cyclo(D-Phe-GWAVGHLL) could be understood through its potential applications and the unique structural properties it boasts. Typically, compounds like this one are explored for their roles in enhancing certain physiological processes or potentially modulating specific biochemical pathways. The cyclic nature of peptides helps them to maintain a particular conformation that could be crucial for binding interactions, which makes them of immense interest in therapeutic and biochemical research settings. They can be used to investigate new drug targets or to develop specialized treatments owing to their affinity and specificity for binding sites that linear peptides and small molecules might not target effectively. Furthermore, Cyclo(D-Phe-GWAVGHLL), like other cyclic peptides, may exhibit a host of bioactivities depending on the context. For instance, certain cyclic peptides are known for their antimicrobial, anticancer, and anti-inflammatory properties. While each specific cyclic peptide, including Cyclo(D-Phe-GWAVGHLL), needs thorough investigation to ascertain its full range of effects, researchers can be hopeful about finding desirable therapeutic or technological applications. In summary, the primary benefits of Cyclo(D-Phe-GWAVGHLL) derive from its structural integrity and the advanced stability conferred by its cyclic nature and the presence of D-amino acids. Although research is ongoing, such peptides hold promise for the development of new therapies and applications in both biomedical and industrial fields due to their unique properties.

How is Cyclo(D-Phe-GWAVGHLL) distinct from other peptides?

Cyclo(D-Phe-GWAVGHLL) is distinctly different from other peptides due primarily to its cyclic structure and the specific inclusion of D-amino acids. To appreciate these differences, consider the general classification of peptides into linear and cyclic varieties. Linear peptides are unbranched sequences of amino acids linked by peptide bonds, akin to proteins but generally shorter in length. These peptides, while abundant in nature and relatively easy to synthesize, often suffer from rapid degradation by proteases in biological contexts and can lack selectivity in their interactions due to their flexibility and linearity. In contrast, Cyclo(D-Phe-GWAVGHLL), as a cyclic peptide, forms a closed loop. This means the N-terminus and C-terminus are linked to each other via chemical bonds, usually peptide bonds or others like disulfide bridges. This cyclic nature imparts a significant degree of rigidity to the peptide structure, often leading to increased thermal and proteolytic stability. Moreover, cyclic peptides like Cyclo(D-Phe-GWAVGHLL) often exhibit a greater potency and selectivity for specific target molecules compared to their linear counterparts because the cyclic structure can mimic key structural motifs required for binding to biologically relevant targets. The integration of D-phenylalanine (D-Phe) adds another layer of distinction. D-amino acids are enantiomers of the more common L-amino acids found in biological systems, and their incorporation is a strategic modification aimed at reducing the susceptibility of peptides to enzymatic degradation. D-amino acids are not easily recognized by most of the enzymes that cleave proteins and peptides, therefore endowing the peptide with a longer functional lifespan when used in biological contexts. Moreover, the presence of D-amino acids can enhance the binding affinity and specificity of Cyclo(D-Phe-GWAVGHLL) for its targets by altering the conformational landscape of the peptide. This is critically important for applications where peptide stability, durability, and target specificity are paramount. Thus, compared to standard linear peptides or those composed solely of L-amino acids, Cyclo(D-Phe-GWAVGHLL) combines the mechanical benefits of a cyclic structure with the biochemical advantages conferred by D-amino acids, making it an intriguing subject for research and development in various scientific fields.

In what fields of research or industries could Cyclo(D-Phe-GWAVGHLL) potentially be used?

Cyclopeptides such as Cyclo(D-Phe-GWAVGHLL) have tremendous versatility and potential across numerous spheres of research and industry due to their unique structural attributes and biochemical properties. The primary fields where Cyclo(D-Phe-GWAVGHLL) could prove to be beneficial include pharmaceuticals, biochemistry, material sciences, and agricultural biotechnology. In pharmaceuticals, cyclic peptides are gaining significant attention for their potential as therapeutic agents. Their ability to selectively bind and modulate protein-protein interactions that are often deemed challenging targets in therapeutic design makes them invaluable. Cyclo(D-Phe-GWAVGHLL), through its stable structure and selective binding properties, could be developed into drugs targeting specific pathological pathways or proteins associated with diseases that have unmet medical needs. These include chronic diseases such as cancer, autoimmune disorders, or neurodegenerative illnesses like Alzheimer's or Parkinson's, where the protein interaction pathways are intricate and require precise modulation. In the realm of biochemistry, Cyclo(D-Phe-GWAVGHLL) can play a critical role in elucidating fundamental biochemical pathways. Because of their specificity, cyclic peptides can be employed as molecular probes to study protein functions within live cells without significantly altering physiological conditions. The insights gained from these studies could propel advancements in understanding cellular processes and mechanisms of disease. Material science is another exciting area where the properties of Cyclo(D-Phe-GWAVGHLL) could be harnessed. Cyclic peptides can serve as building blocks for designing advanced materials with bespoke characteristics, such as self-assembly capabilities, enhanced stability, or responsiveness to environmental cues. Such materials could lead to innovations in drug delivery systems, where the precise release of therapeutic agents is crucial, or in the development of biosensors for diagnostic applications. Lastly, in agricultural biotechnology, cyclic peptides like Cyclo(D-Phe-GWAVGHLL) hold promise in developing sustainable agriculture solutions. They can be engineered to mimic natural plant hormones or function as biopesticides, offering a sustainable and eco-friendly alternative to conventional chemical treatments. Through all these potential applications, the future of Cyclo(D-Phe-GWAVGHLL) and similar compounds looks promising, emphasizing the necessity for continued research and development across multiple scientific disciplines.

What challenges are involved in researching and developing Cyclo(D-Phe-GWAVGHLL)?

Researching and developing Cyclo(D-Phe-GWAVGHLL), like any advanced biomolecular compound, entails several complex challenges that must be surmounted to unlock its full potential. These challenges can be grouped under synthesis and scalability, functional understanding, regulatory hurdles, and translation into practical applications. Firstly, the synthesis of cyclic peptides is more sophisticated than linear peptides due to the requirement to form a covalent link between the N and C termini, effectively cyclizing the peptide. This process demands careful optimization of reaction conditions to avoid undesired side reactions and maximize yields. The inclusion of D-amino acids adds another layer of complexity, as they may influence the synthetic route or the solubility and purification of the final product. Additionally, as research progresses from laboratory-scale synthesis to industrial scalability, maintaining the consistency and purity of Cyclo(D-Phe-GWAVGHLL) while keeping costs manageable is a significant challenge. Second, comprehensively understanding the functional and biological properties of Cyclo(D-Phe-GWAVGHLL) involves meticulous investigation through a variety of biochemical and pharmacological assays. Determining the specific targets, binding affinities, and pharmacokinetics entails extensive in vitro and in vivo studies that can be time-consuming and resource-intensive. This analytical rigor is crucial to delineate the therapeutic potential of Cyclo(D-Phe-GWAVGHLL) and ensure that intended biological effects are observed without unforeseen adverse reactions. The third major challenge is navigating the regulatory landscape that governs the development of new biomolecular products. For any application intended for human health, a stringent array of safety, efficacy, and regulatory compliance assessments must be met according to institutions such as the FDA or EMA. These processes involve rigorous documentation, data reporting, and can take multiple years to complete, underlining the need for significant expertise and investment in ensuring compliance. Finally, the translation of Cyclo(D-Phe-GWAVGHLL) into viable market applications involves interfacing with economic, ethical, and societal considerations. Real-world contexts necessitate successful integration into existing systems, ranging from healthcare delivery mechanisms, agricultural practices to material manufacturing, each of which has its own set of challenges and constraints. Overcoming these challenges demands an interdisciplinary approach combining chemistry, biology, pharmacology, regulatory studies, and business analytics. Such a comprehensive approach not only optimizes the development process but also ensures that this promising compound achieves meaningful utility across various domains.

How does the inclusion of D-Phe in Cyclo(D-Phe-GWAVGHLL) impact its properties compared to conventional peptides?

The inclusion of D-phenylalanine (D-Phe) in Cyclo(D-Phe-GWAVGHLL) substantially influences its properties, differentiating this compound from conventional peptides that rely primarily on L-amino acids. D-amino acids are the enantiomers of the naturally occurring L-amino acids, and their incorporation into peptides leads to profound effects on biological stability, target specificity, and overall bioavailability, oftentimes offering distinct advantages. One of the most critical impacts of including D-Phe in Cyclo(D-Phe-GWAVGHLL) is the enhancement of proteolytic stability. Proteolytic enzymes, which are ubiquitous in biological systems, selectively recognize and cleave L-amino acid containing peptides. By incorporating D-amino acids such as D-Phe, Cyclo(D-Phe-GWAVGHLL) becomes less susceptible to enzymatic degradation. This increased stability is pivotal in therapeutic contexts where extended peptide activity is desired, as it permits the compound to maintain its functional integrity longer within the body, which is often a major hurdle for conventional L-amino acid peptides. Furthermore, the presence of D-Phe influences the conformational landscape of the peptide. D-amino acids introduce a chirality that can modify the peptide's three-dimensional structure, potentially enhancing its binding affinity and specificity for target molecules. This specific interaction is highly beneficial for designing peptides that must precisely interact with particular proteins or cellular receptors, enhancing the efficacy of Cyclo(D-Phe-GWAVGHLL) in targeting diseases with a higher level of precision and reduced off-target effects. Another important consideration impacted by D-Phe is peptide solubility and membrane permeability, both of which are crucial for oral bioavailability and successful systemic delivery. D-amino acids in peptides can sometimes alter these properties, though the overall impact is highly dependent on the specific sequence and structure of the peptide. Tailoring these characteristics can result in better pharmacokinetic profiles compared to conventional peptides. The inclusion of D-Phe also opens pathways for innovative applications beyond therapeutic contexts, such as enabling Cyclo(D-Phe-GWAVGHLL) to serve as a molecular scaffold for materials science applications. Adjusting size, stability, and functionality through stereochemistry changes can lead to the development of novel biomaterials with desirable chemical and physical properties. Hence, the inclusion of D-Phe in Cyclo(D-Phe-GWAVGHLL) is not merely a structural variation but a strategic advancement that provides a foundation for enhanced biological function, stable therapeutic development, and novel material applications. This combination of attributes allows Cyclo(D-Phe-GWAVGHLL) to offer solutions in fields and applications where conventional peptides may fall short.
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