Taiy Chemical
Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur
Synonym PP1-17 (A31,Aib32)-Neur
Species Human
Protein Accession P01296
Purity ≥ 95%
Endotoxin Level < 1.0 EU per µg
Biological Activity Not determined
Expression System Chemical synthesis
Fusion Tag None
Predicted Molecular Mass 2099.4 Da
Formulation Lyophilized from a 0.2 μm filtered solution in 30% acetonitrile and 0.1% TFA
Reconstitution It is recommended to reconstitute the lyophilized product in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted in aqueous solutions as needed
Storage & Stability Store lyophilized product at -20°C. Reconstituted product should be stored at -20°C or below. It is recommended to freeze-thaw once only.
FAQ
What is Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur and how does it work within the body?

Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur is a modified peptide delegate that plays an intricate role in various physiological processes within the body. Typically derived from the pancreatic polypeptide family, this compound is a result of specific amino acid modifications that enhance its activity and stability. The peptide operates primarily in the realm of neuromodulation and metabolic regulation. It is crucial to understand that pancreatic polypeptides are small proteins that contain 36 amino acids, playing multifaceted roles in the regulation of endocrine and exocrine pancreatic secretions, and they help in influencing hepatic glycogen levels.

The specific modification of the molecule, articulated as (1-17)-(Ala31,Aib32), indicates particular alterations at the amino acid positions, resulting in decreased proteolytic degradation. As such, this modification can lead to prolonged half-life and increased efficacy in biological systems. The substitution involving alpha-aminoisobutyric acid (Aib), for instance, confers structural rigidity that results in enhanced biological stability and activity. In the body, this peptide interacts with Y4-receptors, which are G-protein-coupled receptors. Engagement with these receptors influences several neuroendocrine actions and downstream signaling pathways, thus playing a role in adjusting energy balance, food intake, and gastric motility.

This peptide can be critical in research related to mechanisms underlying appetite and weight regulation. It's understood that the manipulation of its signals can provide insight into treating disorders linked to obesity and metabolic dysfunction. It operates via the modulation of certain brain centers involved in hunger and satiety. It also indirectly affects glucose homeostasis by acting upon insulin and glucagon secretion. Facilitating this interaction, the peptide can be key in research situations targeting diabetes management. Through rigorous experimentation, the potential therapeutic implications of Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur emerge, primarily geared toward influencing appetite regulation and metabolic disease management.

What are the primary scientific applications for which Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur is being studied and utilized?

Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur is a focus of study primarily due to its role in modulating several key physiological processes that could translate into therapeutic applications, particularly in the realms of neuroendocrinology and metabolism. A significant portion of research aims to uncover the peptide's involvement in controlling appetite and regulating body weight, presenting potential pathways for addressing obesity. By elucidating the mechanisms that pan out when this peptide interacts with its corresponding receptors, there is considerable promise in uncovering new, targeted therapies that are better at managing excess weight by curbing appetite and modulating energy use. This exploration relies heavily on understanding its interaction with neuropeptide Y-related Y4 receptors in both peripheral tissues and the central nervous system.

Further, there is keen interest in the peptide's ability to manage glucose homeostasis with potential implications for diabetes research. The peptide's influence on pancreatic insulin and glucagon secretion is an attractive feature for developing novel antidiabetic treatments. By acting upon the mechanisms of insulin regulation, it's hypothesized that Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur might help mitigate some of the challenges faced in conventional diabetes treatment paradigms, such as hypoglycemia and insulin resistance. Beyond metabolic implications, this peptide can have broader applications in understanding and potentially managing various gastrointestinal disorders. Given its interaction with gut motility, researchers are investigating how this peptide might be useful in conditions characterized by dysregulated gastric and intestinal movement.

Moreover, in the sphere of academic research, Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur is utilized for elucidating the broader scope of peptide-receptor interaction models. As an area of interest, studies focus on how similar peptide modifications can lead to enhanced specificity and prolonged therapeutic activity, presenting avenues for innovation in the creation of new biomolecules with desired characteristics. By employing this peptide in evidence-driven research, scientists are carving out a deeper understanding of endocrinological homeostasis and its perturbations, offering valuable contributions to both foundational and applied bioscience.

How do the specific modifications present in Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur affect its biological activity and stability?

The modifications present in Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur significantly influence both its biological activity and stability, rendering it more effective for research purposes compared to its unmodified counterparts. Initially, it's important to grasp that peptides are generally susceptible to swift degradation by proteolytic enzymes present in the body, potentially impairing their bioavailability and function after administration. The specific modifications here — replacement at positions Ala31 and Aib32 — impart notable changes to its structure and behavior.

A critical modification is the inclusion of alpha-aminoisobutyric acid (Aib) at the 32nd position. Aib is a non-standard amino acid that provides sterical hindrance, making the peptide less susceptible to enzymatic cleavage. The increased conformational rigidity, thus conferred, not only aids in extending the half-life of the peptide but also ensures that it can withstand metabolic degradation more robustly. This structural fortification ensures that a greater fraction of the peptide remains intact and active upon reaching its site of action, sustaining its biological function for a longer period.

Additionally, the incorporation of alanine and respective substitutions affect the secondary structure of the peptide. These substitutions can promote the formation of stable alpha-helices or reverse-turn structures that are less prone to enzymatic attack, thereby enhancing receptor-binding affinity. Such structural attributes intensify its affinity and specificity for the Y4 receptors, which have far-reaching implications for its potency and efficacy. These modifications enable more precise modulation of physiological pathways, including those that regulate food intake and energy expenditure: the peptide demonstrates improved agonistic properties in its interaction with target receptors, potentially leading to pronounced physiological responses at lower concentration thresholds.

Furthermore, these structural changes may help to modulate the pharmacological profile of the peptide by influencing its absorption, distribution, and excretion dynamics. Enhanced metabolic stability allows for better in vivo tracking to understand pharmacokinetics. Collectively, these modifications to Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur create an advanced, stable analog that has increased potential for understanding peptide-based signaling mechanisms and therapeutic applications. This illustrates how strategic molecular engineering can transform the functional landscape of biological peptides.

What potential therapeutic roles could Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur play in medical science?

Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur holds promise as a potential therapeutic agent across several domains within medical science, primarily due to its role in regulating metabolic and neuroendocrine processes. One of the most exciting areas for its application is in the management of obesity and related metabolic disorders. The peptide's ability to modulate appetite by interacting with neuropeptide Y receptors offers a pathway to mitigate excessive food intake. This interaction effectively informs the central nervous system of satiety, potentially curbing overeating and promoting more controlled weight management. It holds the potential to work synergistically with existing therapeutic strategies to reduce body weight by adjusting the calorie intake with a biological mechanism directly linked to hunger cues.

Furthermore, continued exploration of this peptide could lead to advancements in diabetes management. The peptide's involvement with pancreatic hormone secretion has implications for insulin and glucagon modulation, critical factors in maintaining glucose homeostasis. By enhancing insulin sensitivity or modulating beta-cell function, Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur-based treatments could offer an innovative approach to tackling both type 1 and type 2 diabetes. They could particularly address the challenges of optimizing glucose levels while minimizing side effects like hypoglycemic episodes, offering a refined tool in precision medicine against diabetes.

In addition to its metabolic potential, there is room for therapeutic development concerning gastrointestinal disorders. Given its possible effects on gastric motility, the peptide can be a candidate in treating conditions related to dysregulated peristalsis or gastroparesis. By understanding how the peptide affects smooth muscle contraction in the digestive tract, new interventions could be crafted that alleviate symptoms and enhance life quality for affected individuals.

The modulation of neuroendocrine pathways also opens doors to influence conditions such as stress or anxiety, potentially impacting mental health outcomes. Neuroendocrine interactions that govern stress responses can be altered beneficially, providing another application field. As research progresses, insights gleaned could also impact diseases tied to dysregulated peptide hormone systems, such as Prader-Willi syndrome, an area where appetite regulation is crucial. Through this peptide, the enhancement of receptor selectivity and prolonged activity suggests potential for a wide variety of therapeutic exploits in future pharmaceutical developments. The therapeutic dynamism of Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur continues to be an intriguing journey in the evolution of peptide-based therapy in modern medicine.

What are the challenges and considerations in utilizing Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur for research or therapeutic purposes?

Utilizing Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur for research and therapeutic purposes comes with its own set of challenges and considerations that scientists and medical practitioners must navigate. First and foremost is the complexity involved in optimizing peptide synthesis. Creating such a specifically modified peptide requires high precision in chemical engineering to accurately substitute the desired amino acids. Errors in the synthesis process can result in impurities that alter the peptide’s efficacy and safety. The complexity of these syntheses raises both the cost and time required for laboratory preparation, potentially limiting accessibility and slowing down the pace of research and therapeutic development.

Another challenge lies in the peptide's delivery mechanisms in clinical settings. Peptides generally exhibit poor oral bioavailability due to degradation in the gastrointestinal tract and poor membrane permeability. As a result, alternative delivery routes must be explored, such as intravenous or subcutaneous injections, which can be invasive and may reduce patient compliance. Developing novel delivery systems that protect the peptide from degradation and ensure it reaches its target site effectively is crucial but can be technologically demanding and financially burdensome.

Dosage and safety profiling also pose significant challenges. Establishing the safety of long-term applications of Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur demands comprehensive preclinical and clinical testing phases to avoid adverse effects and toxicity. The peptide's impact on human physiology, given its interactions with several metabolic and neurological pathways, necessitates detailed investigation into any potential off-target effects or unintended consequences, such as hormonal imbalances or immune reactions.

Furthermore, the novelty of modified peptides in therapeutic roles requires extensive education and awareness among healthcare providers. A lack of familiarity can affect their readiness to adopt such innovations, impacting how quickly new treatments could be integrated into clinical practice. These issues are compounded by the regulatory hurdles needed to approve this peptide for therapeutic use, necessitating rigorous evidence and stringent compliance with regulatory standards to ensure pharmaceutical-grade safety and efficacy.

Scientific considerations include maintaining the peptide's stability across storage and handling processes, as improper conditions can lead to degradation and loss of activity. Additionally, when considering the design of clinical trials, researchers must address ethical concerns, such as ensuring informed consent and safeguarding against potential risks associated with experimental treatments.

Overall, while the therapeutic potential of Pancreatic Polypeptide (1-17)-(Ala31,Aib32)-Neur is promising, these challenges require systematic and resourceful approaches to overcome. Collaborative research, investment in advanced peptide delivery technologies, and adherence to regulatory protocols combined with educational outreach constitute vital components of navigating these challenges effectively in the path toward medicinal advancement.
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