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.