Synonym |
(Trp3,Arg5)-Ghrelin (1-5), GSWFR |
Species |
Human |
Protein Accession |
P55056 |
Purity |
> 95% |
Endotoxin Level |
< 1.0 EU per 1 μg of protein |
Biological Activity |
Stimulates the release of growth hormone from the anterior pituitary |
Expression System |
Chemically synthesized |
Fusion Tag |
None |
Predicted Molecular Mass |
684.8 Da |
Formulation |
Lyophilized from a 0.2 μm filtered solution in Acetic Acid and TFA |
Reconstitution |
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml.
|
Storage & Stability |
Store lyophilized protein at -20°C. Reconstituted protein should be stored at -20°C or -80°C.
Avoid repeated freeze-thaw cycles. |
FAQ
What is (Trp3,Arg5)-Ghrelin (1-5), GSWFR, and how does it work in the body?
(Trp3,Arg5)-Ghrelin
(1-5) is a synthetic peptide fragment of the hormone ghrelin, specifically focusing on the first five
amino acids: Gly-Ser-Trp-Phe-Arg (GSWFR). Ghrelin, often referred to as the "hunger hormone," plays a
crucial role in stimulating appetite, regulating energy balance, and promoting growth hormone release.
Produced primarily in the stomach, ghrelin activates receptors in the hypothalamus to signal hunger to
the brain. The (Trp3,Arg5)-Ghrelin (1-5) fragment has been modified at positions 3 and 5 for specific
research purposes to study its physiological effects, including its potential impact on appetite
regulation, metabolism, and growth hormone secretion.
The mechanism of action for ghrelin
involves binding to the growth hormone secretagogue receptor (GHS-R) found in the central nervous system
and peripheral tissues. This interaction not only stimulates hunger but also influences energy
homeostasis and hormone secretion. Studies on (Trp3,Arg5)-Ghrelin (1-5) aim to understand how this
modified peptide affects these complex biological processes. Researchers investigate its role in food
intake behavior, where it mimics or inhibits ghrelin’s natural effects, and its impact on growth
hormone-releasing patterns. Moreover, exploring this peptide's metabolic functions might provide
insights into potential therapeutic applications for conditions such as obesity, cachexia, and metabolic
syndrome.
It's important to note that while (Trp3,Arg5)-Ghrelin (1-5) is promising for scientific
exploration, much of the research is still in early stages. Animal models and cellular studies help
elucidate its effects, but further investigations are needed to determine its efficacy and safety in
humans. Understanding the peptide's pharmacokinetics, bioavailability, and potential side effects
remains a primary focus of ongoing research. The exciting aspect is its focus on the ghrelin pathway,
which opens opportunities to modulate hunger and growth hormone activities, potentially leading to
innovative treatments that address a range of metabolic and endocrine disorders.
What research
supports the use of (Trp3,Arg5)-Ghrelin (1-5) in scientific studies?
The interest in
(Trp3,Arg5)-Ghrelin (1-5) among researchers primarily arises from its derivative nature from ghrelin,
the hormone well-documented for its role in hunger regulation, growth hormone secretion, and energy
balance. Numerous studies have explored ghrelin’s physiological effects, establishing foundational
knowledge crucial for pursuing derivatives like (Trp3,Arg5)-Ghrelin (1-5). A significant body of
preclinical research focuses on the ghrelin pathway’s molecular function to understand how this peptide
fragment could modulate similar or novel outcomes.
Animal model studies, particularly using
rodents, form the bulk of research into (Trp3,Arg5)-Ghrelin (1-5). These studies help elucidate how the
peptide influences behavior and physiology. Researchers often assess its impact on food consumption,
energy expenditure, and hormone levels under controlled conditions. Such experiments aim to unravel
differences between the native ghrelin function and the potentially unique effects of this peptide
variant. Specific alterations in its amino acid structure are hypothesized to offer selective advantages
targeting particular aspects of the ghrelin receptor pathway.
Cellular studies further support
this line of research by allowing scientists to observe biochemical processes in vitro. These settings
enable detailed investigations of receptor binding affinities and subsequent signal transduction
pathways activated by (Trp3,Arg5)-Ghrelin (1-5). By comparing these dynamics with those induced by
endogenous ghrelin, researchers hope to pinpoint precise molecular interactions involved in this
peptide's function. This data may unveil new opportunities for drug development, particularly if
(Trp3,Arg5)-Ghrelin (1-5) demonstrates desirable efficacy and favorable safety
profiles.
Published literature also sheds light on the growing interest in ghrelin analogs like
(Trp3,Arg5)-Ghrelin (1-5). Peer-reviewed articles and conference presentations track advancements in
this domain, pointing to increased collaboration between academia and biotech industries. Such
partnerships are critical as they pool expertise from molecular biology, pharmacology, and clinical
science, contributing to the comprehensive understanding needed to transition from bench research to
potential therapeutic applications. Engaging with ongoing studies and contributing data are essential
steps in realizing the full potential of (Trp3,Arg5)-Ghrelin (1-5) in biomedical research.
What
potential applications does (Trp3,Arg5)-Ghrelin (1-5) have in medical or therapeutic
contexts?
(Trp3,Arg5)-Ghrelin (1-5) holds promise in several therapeutic areas due to its
association with the ghrelin pathway. Primarily, it is of interest in the context of metabolic disorders
such as obesity and cachexia. In obesity treatment, manipulating appetite regulation and energy balance
is crucial. Ghrelin and its derivatives, including (Trp3,Arg5)-Ghrelin (1-5), provide a means to
influence these pathways, potentially offering new strategies to manage excessive weight gain by curbing
appetite without adverse side effects commonly associated with energy metabolism
interventions.
Conversely, in cachexia—characterized by undesired weight loss and muscle wasting
typically associated with chronic diseases like cancer and AIDS—enhancing appetite and anabolic
processes is beneficial. Ghrelin's natural function includes appetite stimulation and promoting growth
hormone release, which are both anabolic factors that could counteract cachexia symptoms. Analogous
peptides that mimic these properties, like (Trp3,Arg5)-Ghrelin (1-5), might stimulate appetite and
improve energy intake, which is critical in maintaining body mass in affected patients.
Beyond
metabolic disorders, (Trp3,Arg5)-Ghrelin (1-5) shows potential in treating growth hormone deficiencies.
Compared to traditional interventions, this peptide, due to its targeted action, might offer an
alternative with fewer side effects. Its action on growth hormone regulation could prove a less invasive
and more physiological method to help individuals with deficient growth hormone
secretion.
Additionally, researchers explore the peptide's neuroprotective capacities. Ghrelin is
known to have roles beyond metabolic regulation, such as influencing cognitive functions and
neuroprotection. Preliminary evidence suggests ghrelin administration might help in neurodegenerative
conditions by providing protective effects within neural tissues. If (Trp3,Arg5)-Ghrelin (1-5) retains
these properties—or optimizes them due to its structure—it could serve as a basis for treating diseases
like Alzheimer's or Parkinson's.
Lastly, the stress-related psychological impacts of ghrelin
pathways provide another potential therapeutic application for this peptide. Regulating the stress
response, especially in conditions like anxiety and depression where ghrelin levels fluctuate, indicates
another frontier awaiting deeper investigation. (Trp3,Arg5)-Ghrelin (1-5)'s selective targeting of
specific receptor pathways could lead to novel treatments addressing mental health disorders with
intricate ties to metabolic status and stress resilience.
Are there any side effects or safety
concerns associated with (Trp3,Arg5)-Ghrelin (1-5)?
As with any bioactive compound under
investigation, it is crucial to thoroughly understand the safety profile and potential side effects of
(Trp3,Arg5)-Ghrelin (1-5). At present, much of the focus is on preclinical studies, mainly involving
animal models, to determine its tolerability, pharmacodynamics, and pharmacokinetics. In these early
stages, researchers are examining common parameters such as toxicity, adverse reactions, and long-term
effects to establish a comprehensive safety profile.
Considering ghrelin's primary role in hunger
regulation, potential side effects could include changes in appetite and body weight, though the
modified nature of (Trp3,Arg5)-Ghrelin (1-5) might mitigate these effects or alter them in potentially
beneficial ways. Unintended stimulation or suppression of hunger could lead to weight gain or loss,
respectively. Therefore, understanding how this peptide modulates the hunger pathway is essential to
predicting and managing these outcomes.
Hormonal interactions are another area of concern, given
ghrelin's role in growth hormone secretion. An imbalance resulting from excessive or inadequate growth
hormone levels could lead to metabolic disturbances, growth abnormalities, or endocrine disorders.
Animal studies help map these hormonal fluctuations under controlled dosages, providing insights into
potential risks.
Moreover, cardiovascular implications must be considered, as ghrelin and its
analogs can exert cardiovascular effects, including changes in blood pressure and heart rate. Monitoring
these parameters during experimental trials ensures any adverse cardiovascular reactions are documented
and understood.
Allergic reactions or immunogenicity remain potential risks with peptide-based
therapies. The body's immune response to administered peptides sometimes results in hypersensitivity;
thus, observing for such reactions is part of the standard procedure in preclinical
research.
Researchers are also cautious about potential central nervous system (CNS)
effects—considering the peptide’s interaction with CNS receptors—monitoring for behavioral changes or
neuropsychiatric effects due to its administration. Such vigilance helps prevent unintended impacts on
cognition or mood.
Ultimately, while the promise of (Trp3,Arg5)-Ghrelin (1-5) in therapeutic
contexts is clear, researchers must meticulously address safety and side effects throughout its
development. As research progresses toward human trials, these concerns are further investigated through
rigorous clinical testing to ensure safe application.
How is (Trp3,Arg5)-Ghrelin (1-5)
synthesized, and what challenges are faced in its production?
The synthesis of
(Trp3,Arg5)-Ghrelin (1-5) involves the assembly of its specific peptide sequence, Gly-Ser-Trp-Phe-Arg,
using contemporary peptide synthesis techniques. This process typically employs solid-phase peptide
synthesis (SPPS), a popular method for constructing peptides. In SPPS, the peptide is assembled one
amino acid at a time while tethered to a solid resin support, allowing for sequential addition through
carefully controlled chemical reactions.
Amino acids are added in a defined order, with each
cycle involving three main steps: deprotection, coupling, and washing. First, the protecting group on
the growing peptide chain—commonly Fmoc (fluorenylmethyloxycarbonyl)—is removed to allow the next amino
acid to bind. Then, the newly deprotected terminal is coupled with the activated amino acid derivative.
Finally, the peptide-resin complex is washed to remove excess reagents and by-products. This cycle
repeats, meticulously forming the peptide’s sequence.
Producing (Trp3,Arg5)-Ghrelin (1-5) also
necessitates fidelity in incorporating modified amino acids—such as Trp and Arg modifications tailored
to its function. This requires refined synthesis strategies and precision in reagent selection to
achieve the desired modification without compromising peptide integrity.
One of the main
challenges in synthesizing (Trp3,Arg5)-Ghrelin (1-5) lies in maintaining high purity and yield,
particularly given the modified residues. These modifications affect the peptide’s chemical properties,
potentially leading to aggregation or improper folding, complicating purification processes. Advanced
techniques such as high-performance liquid chromatography (HPLC) help isolate the target peptide from
impurities.
Scale is another challenge, as moving from bench-scale to commercial-scale synthesis
without losing efficiency or purity requires adept process optimization. Additionally, ensuring the
peptide’s stability during production and storage is critical; thus, lyophilization and specific storage
conditions are employed to preserve functionality.
Continued innovation in peptide synthesis aims
to overcome these challenges; efforts include developing automated synthesizers and enhancing
purification technologies to improve scalability and efficiency. Despite these hurdles, the synthesis of
(Trp3,Arg5)-Ghrelin (1-5) remains feasible, facilitating its availability for research and potential
therapeutic development.