Synonym |
Cyclo(Glu22-Lys26),Leu27-pTH (1-31) amide (hum |
Species |
Human |
Protein Accession |
NA |
Purity |
NA |
Endotoxin Level |
NA |
Biological Activity |
NA |
Expression System |
NA |
Fusion Tag |
NA |
Predicted Molecular Mass |
NA |
Formulation |
NA |
Reconstitution |
NA |
Storage & Stability |
NA |
FAQ
What is the primary function of (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum) in scientific
research?
The peptide known as (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum) is designed to
study its interaction with the parathyroid hormone (PTH) receptor. This molecule is a modified version
of the native parathyroid hormone, featuring alterations such as cyclization and amide modifications,
which can change its binding properties and stability. By understanding the behavior of this synthesized
peptide, researchers aim to gain insights into the physiological and pathological roles of the
parathyroid hormone in the body. Specifically, the modifications in this peptide help scientists
investigate receptor dynamics and signal transduction pathways that are influenced by PTH. This focus is
crucial for developing therapeutic strategies to treat diseases like osteoporosis and other metabolic
bone disorders, where PTH plays a pivotal role. Understanding how PTH and its analogs interact with
receptors can lead to advancements in drug design and the development of more effective therapeutic
agents with minimized side effects.
How does (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum)
differ from the natural parathyroid hormone?
The synthetic peptide (Cyclo(Glu22-Lys26),Leu27)-pTH
(1-31) amide (hum) represents a designed alteration of the natural parathyroid hormone, which enables
scientists to explore its structure-function relationships more deeply. The primary difference lies in
the cyclization between Glu22 and Lys26 and the substitution of Leu27. These specific modifications are
designed to alter the peptide's physico-chemical properties, such as increasing its resistance to
enzymatic degradation, which can be a significant hurdle in therapeutic applications of peptides. The
cyclization results in a more compact and potentially more stable three-dimensional structure, offering
researchers a version of PTH that can potentially engage with its receptor in a distinct manner compared
to the natural hormone. Additionally, the amide bond modification at the terminal could enhance the
peptide's bioactivity by prolonging its half-life and maintaining receptor interaction. These slight but
significant changes can yield elaborate insights into how specific structural components of the hormone
influence its activity at the molecular level, possibly leading to innovative applications in treating
conditions that involve PTH regulation.
In what ways can (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31)
amide (hum) contribute to medical advancements?
The research and development of
(Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum) could have significant implications for medical
science, particularly in the realm of treating bone-related diseases. This peptide can serve as a
powerful tool in understanding PTH receptor interactions, filling gaps in current knowledge about
receptor binding and signaling specifics. This understanding is essential for creating more targeted
pharmaceutical interventions for bone metabolic disorders like osteoporosis. As researchers develop an
in-depth understanding of this analog's mechanism of action, it can guide the design of novel drugs that
mimic or inhibit the hormone's natural functions in a more controlled and selective manner, reducing the
risk of side effects associated with broad-spectrum or less specific treatments. Moreover, the insights
gained from studying this molecule can transcend to other areas of endocrine research, potentially
revealing novel therapeutic targets and methodologies. There may also be possibilities of using modified
PTH analogs in regenerative medicine, helping to repair damaged tissues by exploiting their
growth-promoting properties.
Could (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum) be used to
replace traditional hormone therapies?
While (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum) holds
significant promise, its role as a replacement for traditional hormone therapies requires careful
consideration and extensive clinical trials. Its design primarily serves as a research tool to enrich
our understanding of PTH-related pathways. However, its potential for clinical use is substantial,
particularly in creating more effective and targeted therapies with fewer side effects. By providing
more precise control over receptor interactions due to its modified structure, this peptide may enable
more specific therapeutic outcomes, which is a key advantage over traditional PTH or PTH-related
therapies that might not discriminate as effectively between different cellular pathways or receptor
subtypes. Moreover, the stability and activity enhancements aimed by the modifications in this peptide
could translate into longer-lasting therapeutic effects or reduced dosage requirements, proving
beneficial in clinical scenarios. Nonetheless, translating these theoretical benefits into practice
involves a comprehensive assessment of safety, efficacy, and long-term impacts.
What are the
potential side effects of using (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide (hum)?
As a molecular
entity still under investigation, the safety profile of (Cyclo(Glu22-Lys26),Leu27)-pTH (1-31) amide
(hum) remains to be fully characterized. However, given its derivation from parathyroid hormone analogs,
it may share similar side effect profiles found in PTH-based treatments unless the modifications confer
significantly altered pharmacodynamics. Common concerns with PTH analogs include hypercalcemia, where
increased serum calcium levels lead to complications if not carefully monitored and managed. Skeletal
repercussions are also noteworthy; while the goal is typically to enhance bone formation, imbalances can
sometimes lead to potential resorption. Modifications in the peptide's structure may reduce these risks,
either by lowering receptor activation levels or by altering the durations and types of receptor
interactions. However, unforeseen immunogenic reactions triggered by its modified structures or
long-term effects on tissues shouldn't be underestimated. Any practical application of this peptide in a
clinical setting necessitates extensive research to understand its full spectrum of biological
activities and potential adverse effects, which can inform appropriate dosing regimens and safety
monitoring strategies for future therapeutic use.