Synonym |
CGH |
Species |
Human |
Protein Accession |
P38646 |
Purity |
Greater than 95% |
Endotoxin Level |
Less than 1 EU/µg |
Biological Activity |
Stimulates the release of prostaglandin E2 from fibroblasts |
Expression System |
E. coli |
Fusion Tag |
None |
Predicted Molecular Mass |
3147 Da |
Formulation |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA |
Reconstitution |
Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the
sides of the vial to ensure full recovery of the protein into solution |
Storage & Stability |
Store at -20°C. For long-term storage, aliquot and store at -20°C or -80°C. Avoid repeated
freeze-thaw cycles. |
FAQ
What is Cyclo(Gly-His) and how does it work within the body?
Cyclo(Gly-His), known as
Cyclo(Histidyl-Glycine) is a cyclic dipeptide composed of the amino acids glycine and histidine. Cyclic
peptides like Cyclo(Gly-His) have garnered attention for their potential biological activities. In
recent years, there has been increasing scientific interest in these molecules due to their stability
compared to their linear counterparts. The cyclic nature often makes them more resistant to enzymatic
degradation, thereby extending their biological half-life and efficacy within the body.
Once
administered, Cyclo(Gly-His) is believed to interact with various biological pathways. Research suggests
cyclic peptides might play a role in modulating neuroprotective activities. They may influence
neurotransmitter modulation, potentially contributing to cognitive processes, although more research is
necessary to fully understand these interactions. Another area where Cyclo(Gly-His) could be impactful
is its potential role in antioxidant mechanisms. These peptides may interact with free radicals or
contribute to signaling pathways that support the body in maintaining oxidative balance, which is
crucial for cellular health and longevity.
Further exploration into Cyclo(Gly-His) might reveal
its potential in supporting metabolic regulations. Cyclo(His-Pro), closely related to Cyclo(Gly-His),
has shown promise in modulating insulin-related processes, although specific research into
Cyclo(Gly-His) will still be needed to determine whether it shares these benefits. By enhancing our
understanding of how Cyclo(Gly-His) works within the body, we lay the groundwork for future
applications, whether they be in nutritional supplements or therapeutic contexts.
Given the
evolving nature of peptide research, the scientific community continues to explore the potentials and
limits of Cyclo(Gly-His). Advanced studies are required to determine its safety, efficacy, and the
contexts under which it might be most beneficial. While we have hypotheses based on the behavior of
similar peptides, definitive actions and applications of Cyclo(Gly-His) will depend on the outcomes of
ongoing research. For those interested in the intricacies of molecular biology, staying abreast of
research regarding cyclic peptides like Cyclo(Gly-His) offers exciting insights into developing new
strategies for supporting human health.
What potential benefits does Cyclo(Gly-His)
offer?
Cyclo(Gly-His) may provide a range of potential benefits due to its unique cyclic
structure and the biological activities of its amino acid components, glycine and histidine. Though
research is still developing, initial studies on cyclic peptides suggest several promising health
implications, which we can explore to understand the broader context of Cyclo(Gly-His)'s impact on
wellness. One area of interest is the potential neuroprotective benefits. Cyclic peptides are receiving
attention in the field of neuroscience, with preliminary data indicating they might be supportive in
cognitive enhancement and neuroprotection. Cyclo(Gly-His) itself may interact with pathways that
influence neurotransmitter release or brain plasticity, suggesting its utility in supporting cognitive
functions. However, dedicated studies focusing on Cyclo(Gly-His) will be essential to confirm such
effects.
Antioxidant properties represent another promising line of inquiry. Cyclic peptides are
often investigated for their ability to combat oxidative stress, a significant factor in numerous
chronic diseases and aging. By potentially reducing oxidative damage through direct interaction with
reactive oxygen species or by enhancing endogenous antioxidant pathways, Cyclo(Gly-His) could support
cellular health, promoting longevity and overall wellness. Furthermore, since histidine is known for its
role in buffering against excess acidity and potentially influencing metal ion homeostasis,
Cyclo(Gly-His) might share similar capabilities, lending it a role in maintaining metabolic stability
and cellular function.
Moreover, the peptide may aid in metabolic regulation. While a bulk of the
existing studies have focused on Cyclo(His-Pro) for insights into insulin function and glucose
tolerance, there's potential that Cyclo(Gly-His) could also support metabolic health. This benefit, if
confirmed through rigorous studies, could aid in addressing metabolic disorders or supporting weight
management strategies.
While the aforementioned potential benefits point to a positive outlook
for Cyclo(Gly-His), it's crucial to underscore that much of this is hypothetical, based on the
properties of related compounds. To solidify these claims, scientific investigations are essential.
These should include clinical trials to assess efficacy, safety, and dosage recommendations. Until then,
Cyclo(Gly-His) should be viewed through a lens of cautious optimism, recognizing its potential while
acknowledging the need for ongoing research.
Are there any side effects or risks associated with
Cyclo(Gly-His)?
Currently, there is limited specific data on the side effects or risks directly
associated with Cyclo(Gly-His). As with many peptides, more comprehensive studies and clinical trials
are needed to fully ascertain any potential adverse effects. Peptides, owing to their nature as short
chains of amino acids, are typically considered to have fewer side effects compared to synthetic
pharmaceuticals. However, this does not completely eliminate the possibility of side effects or risks
associated with their use.
General risks with peptide-like substances can include allergic
reactions, although such cases are rare. It is important to ensure that any peptides used in food
supplements or therapeutic applications are of high purity and quality to minimize this risk. Impurities
that might arise during synthesis or formulation could potentially elicit undesired immune responses.
Any adverse reactions should be reported to a healthcare professional for evaluation.
Given the
emerging nature of peptide research, and Cyclo(Gly-His) in particular, potential long-term effects
remain to be seen. The human body might metabolize peptides, but studies are needed to confirm how
Cyclo(Gly-His) behaves over prolonged periods and whether any metabolites produced pose any risk.
Therefore, continuous monitoring and updating safety profiles based on longitudinal studies will be
necessary as the understanding of Cyclo(Gly-His) evolves.
Furthermore, interactions with
medications or other supplements could present concerns. Peptides sometimes influence biochemical
pathways significantly, hence, they might interact with medications that modulate similar processes.
Therefore, it is essential for users to consult healthcare professionals, especially if they are under
medication, to evaluate potential interactions.
Adhering to recommended dosages, once
established, is crucial to minimizing risk. Overdosage, while uncommon with peptides, could
theoretically lead to unforeseen complications given the potential biochemical impacts of
Cyclo(Gly-His).
In summary, while Cyclo(Gly-His) holds promise in various health-related
applications, until substantive clinical research is available, cautious use under professional guidance
is always prudent. Future studies will likely provide more detailed information on safety, including
potential side effects, contraindications, and guidelines for safe use in diverse
populations.
How is Cyclo(Gly-His) different from other cyclic peptides?
Cyclo(Gly-His) is
unique due to its specific amino acid composition and the potential functions it might perform in
biological systems. Like other cyclic peptides, it boasts enhanced stability compared to linear peptidic
structures, resulting in potential benefits in biochemical resilience and sustained activity. The cyclic
configuration shields the peptide bond from proteolytic enzymes, thus preventing premature degradation,
which is a common challenge faced by linear peptides. This feature potentially gives Cyclo(Gly-His) a
prolonged half-life, enhancing its bioavailability and maintaining its functional presence longer within
the body.
What sets Cyclo(Gly-His) apart is primarily the combination of glycine and histidine.
Glycine, the simplest amino acid, contributes to structural flexibility and is often involved in diverse
biological functions, including neurotransmission and antioxidant processes. Histidine, on the other
hand, is known for its buffering capacity, its role in metal ion chelation, and its influence on enzyme
activity. When combined in the cyclic structure of Cyclo(Gly-His), these two amino acids may participate
in unique interactions with biological molecules, differing from those of other cyclic peptides with
different amino acid compositions.
While Cyclo(His-Pro) has been extensively studied for its
potential metabolic benefits, Cyclo(Gly-His) may offer insights into other areas, such as
neuroprotection, owing to the intriguing roles of its constituent amino acids in brain health and
neurotransmission. It is also worth noting that despite possible similarities with other cyclic
dipeptides, the specific reactive centers and molecular interactions attributed to Cyclo(Gly-His)
contribute to a distinct profile that requires its own set of investigations.
Furthermore, the
peptide's distinct structure may influence the pathways it engages with and its functions once within a
biological system. While the cyclic nature provides structural advantages, the unique amino acid pair
can lead to different binding affinities, target interactions, and overall physiological effects. Each
cyclic peptide, including Cyclo(Gly-His), can exhibit specificity for certain receptors or enzymes,
differentiating their potential therapeutic uses.
In summary, while Cyclo(Gly-His) shares the
cyclic nature with other peptides, its distinct amino acid combination and resultant biological
interactions set it apart. Continued research is important to further delineate these differences and
explore the specific applications and advantages that Cyclo(Gly-His) may offer in scientific and
medicinal contexts.
What are the methods used for synthesizing
Cyclo(Gly-His)?
Synthesizing Cyclo(Gly-His) involves creating a cyclic dipeptide by connecting
the amino acids glycine and histidine in a cyclic bond. Typically, synthesizing cyclic peptides poses
certain challenges due to potential issues such as poor yields or racemization, making the choice of
synthesis method critical to obtaining high purity and yields of the desired cyclo-dipeptide. There are
several methods employed for synthesizing cyclic peptides, each with its own set of advantages and
considerations.
One common approach is solution-phase synthesis. This method fundamentally
involves dissolving the amino acids in a suitable solvent, subsequently facilitating the peptide bond
formation through chemical reactions. The cyclization usually requires the activation of one carboxyl
group to form an amide bond with an amino group. However, challenges such as racemization, where
stereochemistry of amino acids might be compromised, are pertinent and care must be taken to minimize
it. Protecting groups might be used during these steps to prevent unwanted side reactions or
racemization, later removed once the cyclization process is complete.
Solid-phase peptide
synthesis (SPPS) is another widely used method due to its ability to simplify purification processes. In
SPPS, the peptide chain is anchored to an insoluble resin, allowing for sequential addition of amino
acids. Cyclization can occur on the solid support or after the peptide is cleaved from the resin. SPPS
benefits from the ease of purification, where unreacted or by-product impurities are washed away, and
the process is often more conducive to automation, making it suitable for producing small to
medium-sized peptide libraries for research and development.
Enzymatic methods have emerged as
greener alternatives, utilizing enzymes to catalyze the formation of the cyclic peptide. This approach
is attractive due to its specificity and mild reaction conditions, which can further minimize
racemization and the need for extensive purification steps. However, finding the right enzyme and
optimizing reaction conditions for Cyclo(Gly-His) specifically remains challenging and may not always be
feasible for large-scale production.
Chemical synthesis methods continue to evolve, with
strategies focusing on overcoming traditional limitations related to yield, racemization, and
purification. Advances in catalytic methodologies or coupling reactions continue to improve the
synthesis of cyclic peptides like Cyclo(Gly-His). As the fields of organic and medicinal chemistry
progress, new and more efficient methods are likely to emerge, facilitating the broader application and
study of cyclic peptides in various research and therapeutic domains.