Synonym |
Cyclo(Arg-Ala-Asp-d-Phe-Val) |
Species |
Human |
Protein Accession |
NA |
Purity |
≥ 95% |
Endotoxin Level |
< 0.1 EU/µg |
Biological Activity |
NA |
Expression System |
Chemical Synthesis |
Fusion Tag |
NA |
Predicted Molecular Mass |
NA |
Formulation |
Supplied as a lyophilized powder |
Reconstitution |
Centrifuge vial before opening. Reconstitute in water |
Storage & Stability |
Store at -20°C. Stable for up to 12 months |
FAQ
What is cyclo(-Arg-Ala-Asp-d-Phe-Val) and how does it work in the
body?
Cyclo(-Arg-Ala-Asp-d-Phe-Val) is a type of cyclic peptide, which is a short sequence of
amino acids linked together in a ring structure as opposed to the more conventional linear form seen in
many proteins. This peptide is part of a class of molecules designed to target specific biological
mechanisms, often involved in signaling or interaction between cells. The specific structure of
cyclo(-Arg-Ala-Asp-d-Phe-Val) allows it to attach to particular proteins or receptors, influencing
various biological pathways within the body. By binding to these proteins, it can modulate their
activity, enhancing or inhibiting certain signaling pathways depending on the intended therapeutic
effect.
One of the key advantages of cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val) is their
enhanced stability compared to linear peptides, as the cyclic nature provides a rigid structure that can
resist degradation by enzymes more effectively. This particular peptide may mimic certain natural
ligands that interact with receptor proteins, potentially providing agonistic or antagonistic
interactions that can be used to alter physiological responses. For instance, if it binds to a cell
surface receptor, it could either initiate a cascade of cell signaling events or inhibit the natural
ligand's binding, thus preventing such events.
Research is often focused on its potential
application in various therapeutic areas, such as autoimmune disorders, cancer, or cardiovascular
diseases, where it might influence disease progression or symptom management through its targeted
interactions. The precise pharmacodynamics and pharmacokinetics of the peptide, including how it is
absorbed, distributed, metabolized, and excreted in the body, are critical to its effectiveness as a
therapeutic agent. These characteristics are heavily researched to harness the peptide’s potential
fully. While still under study, such molecules hold promise for advancing precision medicine, providing
more targeted and efficient treatment approaches.
What potential therapeutic applications does
cyclo(-Arg-Ala-Asp-d-Phe-Val) have?
Cyclo(-Arg-Ala-Asp-d-Phe-Val) is being investigated for
several potential therapeutic applications owing to its unique biochemical properties. The peptide's
specific sequence allows it to bind to receptors with high affinity and specificity, which can be
crucial in developing treatments where precise targeting is necessary to modulate biological responses.
One area of interest is cancer therapy. In oncology, this peptide could be utilized to inhibit tumor
growth by targeting integrins, which are proteins involved in cell adhesion and migration. The binding
of cyclo(-Arg-Ala-Asp-d-Phe-Val) to specific integrins could disrupt tumor angiogenesis — the process by
which new blood vessels form to feed tumorous growths — thus starving the tumor of nutrients and
inhibiting its expansion.
In autoimmune disease research, cyclo(-Arg-Ala-Asp-d-Phe-Val) may be
applied to regulate immune responses. Autoimmune disorders occur when the body's immune system
mistakenly attacks its own tissues. By interfering with specific immune cell pathways, the peptide might
be able to reduce these inappropriate immune responses, thereby alleviating disease symptoms and
progression. This targeted modulation can prove particularly beneficial compared to traditional
immunosuppressive therapies that often carry broad side effects due to their lack of
specificity.
Furthermore, cardiovascular diseases might benefit from the action of
cyclo(-Arg-Ala-Asp-d-Phe-Val) by influencing processes such as atherosclerosis or thrombosis. By
regulating cell adhesion and migration within blood vessels, the peptide could potentially prevent the
buildup of plaques or clots that lead to heart attacks or strokes. Other promising areas include wound
healing and regenerative medicine, where the peptide's properties could accelerate recovery by promoting
proper cellular interactions essential for tissue repair.
Overall, the versatility of
cyclo(-Arg-Ala-Asp-d-Phe-Val) across a wide spectrum of diseases underscores the importance of
continuing research to fully elucidate its therapeutic potential. Its ability to offer alternative
treatment options with potentially fewer side effects emphasizes its significance in developing
next-generation pharmaceuticals.
What makes cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val)
preferable to linear peptides in drug development?
The preference for cyclic peptides like
cyclo(-Arg-Ala-Asp-d-Phe-Val) over linear peptides in drug development is attributed primarily to their
enhanced stability, bioavailability, and functional specificity. The cyclic conformation confers a more
rigid structure to the peptide than its linear counterparts, significantly reducing its susceptibility
to enzymatic degradation. This resistance is crucial when the peptide is introduced into a challenging
environment like the human body, where proteases constantly break down peptides and proteins. As a
result, cyclic peptides maintain their integrity longer, providing sustained therapeutic activity, which
is advantageous for efficient drug delivery and prolonged bioavailability in systemic
circulation.
Moreover, cyclic peptides boast a unique ability for fine-tuning selectivity due to
their constrained structure. The fixed spatial arrangement of their amino acid residues often results in
high-affinity binding to specific biological targets, such as enzymes or receptors, implicating a
reduced likelihood of off-target effects that can lead to adverse reactions. For instance,
cyclo(-Arg-Ala-Asp-d-Phe-Val) can precisely interact with particular receptor sites, avoiding
non-specific interactions and reducing undesirable side effects. This specificity is not just beneficial
for enhancing therapeutic efficacy but also serves to improve the overall safety profile of the
drug.
Furthermore, due to their significant polarity and bulk, cyclic peptides often have limited
immunogenicity compared to larger protein-based therapeutics. This reduced antigenicity means that
cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val) are less likely to trigger immune responses within
patients, a complication that can compromise treatment safety and efficacy. They also offer advantages
in terms of pharmacokinetics. The cyclic structure can help improve membrane permeability, allowing
peptides to traverse cellular membranes more effectively than linear peptides, which enhances absorption
and maximizes therapeutic effect.
Cyclic peptides also offer flexibility in terms of chemical
modifications that can be tailored to adjust their pharmacological profile further — optimizing aspects
like solubility, stability, and target affinity. This tunability is invaluable in drug design, providing
an adaptable framework for overcoming limitations inherent in traditional small-molecule drugs or
biologics. Consequently, cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val) have garnered significant
attention not only for their therapeutic capabilities but also for offering a promising platform for
developing more effective and sophisticated drugs.
How is the stability of
cyclo(-Arg-Ala-Asp-d-Phe-Val) beneficial for its use in therapeutic applications?
The stability
of cyclo(-Arg-Ala-Asp-d-Phe-Val) is a critical factor that enhances its suitability for therapeutic
applications. One of the primary advantages of this peptide’s stability is its resistance to enzymatic
degradation, a major limitation encountered by conventional peptide therapeutics. In the human body,
enzymes, particularly proteases, are proficient at breaking down peptide bonds, rapidly degrading linear
peptides and reducing their efficacy. However, the cyclic nature of cyclo(-Arg-Ala-Asp-d-Phe-Val)
provides a conformational rigidity that makes it less susceptible to proteolytic cleavage. This
stability is paramount for maintaining the peptide's bioactivity for extended durations, ensuring that
it can exert its therapeutic effect once administered.
Another significant benefit of the
enhanced stability is improved pharmacokinetic properties. The resistance to degradation extends the
half-life of the peptide in vivo, allowing it to remain in systemic circulation for longer periods. This
prolonged presence not only ensures a sustained action but also allows for potentially less frequent
dosing regimens, improving patient compliance and convenience. For patients, fewer injections or doses
translate into a more manageable treatment schedule, enhancing overall treatment adherence and
success.
The stability of cyclo(-Arg-Ala-Asp-d-Phe-Val) also plays an essential role in its
transport and delivery to targeted tissues. Due to its robust structure, the peptide can be formulated
in various delivery systems without losing its active conformation. This adaptability allows for the
development of dosage forms that can efficiently navigate biological barriers, such as crossing cellular
membranes or the blood-brain barrier if needed, ensuring that the therapeutic agent reaches its intended
site of action.
Furthermore, increased stability ensures that the peptide maintains its
structural integrity under different physiological conditions, such as varying pH levels encountered in
the gastrointestinal tract or bloodstream. Consequently, orally administered cyclic peptides like
cyclo(-Arg-Ala-Asp-d-Phe-Val) could potentially avoid premature degradation, optimizing absorption into
the bloodstream and enhancing therapeutic outcomes. Stability is also a key consideration for storage
and shelf-life of pharmaceutical formulations; cyclic peptides tend to have a longer shelf life,
reducing wastage and ensuring a reliable supply to healthcare providers and patients.
In essence,
the stability of cyclo(-Arg-Ala-Asp-d-Phe-Val) provides a robust platform for developing effective
therapeutic agents that can overcome many of the limitations faced by conventional small molecules and
linear peptides in drug development, paving the way for more precise and efficient
treatments.
What challenges exist in the development and use of cyclo(-Arg-Ala-Asp-d-Phe-Val) as
a therapeutic agent?
Despite the promising attributes of cyclo(-Arg-Ala-Asp-d-Phe-Val) as a
therapeutic agent, several challenges persist in its development and utilization. One significant
challenge is the production and synthesis of cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val). The
synthesis of these peptides often requires complex chemical processes that can be costly and
time-consuming. Ensuring the precise formation of the cyclic structure while maintaining the desired
sequence and stereochemistry demands advanced techniques and high levels of precision. This complexity
in manufacturing not only drives up production costs, making the final therapeutic product more
expensive, but also can impact scalability and the feasibility of wide-ranging clinical
production.
Additionally, cyclic peptides face challenges related to pharmacokinetics and
delivery. Though more stable than linear peptides, cyclic peptides may still face hurdles in efficiently
crossing certain biological barriers. Depending on their size and hydrophobic nature, they may require
specialized delivery systems to ensure they reach their intended target sites within the body. In some
cases, to enhance bioavailability, innovative drug delivery systems must be developed, which can further
complicate the formulation process and require rigorous testing to demonstrate safety and
efficacy.
Another challenge is the potential for immunogenicity. While cyclic peptides are often
less immunogenic than full proteins, they can still evoke an immune response in some individuals. The
potential development of antibodies against the peptide could reduce its effectiveness and increase the
risk of adverse immune reactions. Hence, a thorough understanding of the immune system's response to the
peptide is critical to mitigate any potential negative effects, necessitating extensive preclinical and
clinical studies which increase the timeline and cost for development.
Furthermore, despite their
benefits, cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val) are yet to be comprehensively tested in all
potential therapeutic areas. This creates a gap in the detailed understanding of their long-term
effects, efficacy across different patient populations, and possible drug-drug interactions. These gaps
require intensive research and trials, necessitating collaboration between research institutions,
regulatory bodies, and industry stakeholders to ensure comprehensive assessments.
Lastly, market
acceptance can be a challenge, as healthcare providers and patients transition from established
therapies to novel peptide-based treatments. This requires not just clinical proof of superiority or
equivalent efficacy but also extensive educational efforts to inform stakeholders about the novel
treatment's benefits, safety profile, and application scenarios.
All these challenges highlight
the intensive effort required to bring cyclic peptides like cyclo(-Arg-Ala-Asp-d-Phe-Val) from concept
to clinical reality, underscoring the need for continued research and innovation in overcoming these
obstacles.