Taiy Chemical
(Trp3,Arg5)-Ghrelin (1-5), GSWFR
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.
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