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.