Synonym |
LSKL-NH2 |
Species |
Human |
Protein Accession |
N/A |
Purity |
Greater than 95% as determined by HPLC |
Endotoxin Level |
Less than 1 EU/ug |
Biological Activity |
N/A |
Expression System |
Chemical synthesis |
Fusion Tag |
None |
Predicted Molecular Mass |
1025.18 Da |
Formulation |
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA |
Reconstitution |
It is recommended to reconstitute the lyophilized product with sterile water at a concentration
of 0.1 mg/ml, which can then be further diluted to other aqueous solutions. |
Storage & Stability |
Store lyophilized product at -20°C. Once reconstituted, can be stored at 4°C for up to 7 days.
For long-term storage, aliquot and store at -20°C. |
FAQ
What is LSKL-NH2 and how does it work?
LSKL-NH2 is a modified peptide known in scientific research
for its potential roles in biochemical processes. Peptides are short chains of amino acids, which are
the building blocks of proteins, and they often function as signaling molecules or biological catalysts.
The modification of peptides with terminal groups like "NH2" (an amine group) involves altering its
chemical structure to influence its stability, activity, and interaction with biological molecules. This
modification is intended to enhance the peptide's functionality, making it more suitable for various
applications in research or therapeutic contexts. The essence of peptides like LSKL-NH2 lies in their
ability to interact with cellular receptors, enzymes, or other bioactive molecules, thus influencing
specific signaling pathways. For example, some peptides act as inhibitors or activators of enzymes,
playing critical roles in processes such as cell growth, inflammation, and wound healing. Peptides are
also known for their targeted approach, which is why they are often refined for specific purposes.
LSKL-NH2 may thus be explored for its potential in moderating certain physiological responses.
Scientists often explore peptides like LSKL-NH2 for their therapeutic efficacy, biodegradability, and
reduced toxicity profiles compared to larger protein-based therapeutics. The specificity with which they
interact with their targets can help in designing treatments that minimize off-target effects. Moreover,
the relatively small size of peptides makes them more amenable to chemical synthesis and modification,
allowing researchers to fine-tune their properties for optimal activity and stability in the body. Given
the biological significance of peptides, scientific interest in molecules like LSKL-NH2 is high, as they
promise targeted and effective interventions in various fields of medicine, including oncology,
neurology, and regenerative medicine.
What potential medical applications could LSKL-NH2 have?
Peptides such as LSKL-NH2 hold significant promise in the field of medicine, thanks to their
specific mechanism of action and modifiable nature. In therapeutic contexts, these peptides can be
tailored to bind particular protein targets with high specificity, potentially leading to the
development of treatments for various conditions. One such application could be in targeting fibrotic
diseases. Fibrosis is characterized by the excessive formation of fibrous tissues, leading to impaired
function of affected organs. Peptides like LSKL-NH2 might interact with molecules involved in the
fibrotic process, potentially offering a means to moderate or inhibit fibrosis progression. Another area
of interest is in cancer research. Peptides can be designed to specifically recognize cancer cells or
molecules that are over-expressed in tumors, providing a targeted approach to deliver cytotoxic agents
directly to cancer cells, minimizing damage to healthy cells. This makes peptides an exciting tool in
the development of cancer therapeutics or imaging agents. In inflammation-related conditions, peptides
such as LSKL-NH2 could be explored as therapeutic agents due to their potential to modulate immune
responses. This involves downregulating pro-inflammatory cytokines or inhibiting pathways that lead to
chronic inflammation, thus providing potential symptomatic relief or disease-modifying effects in
chronic inflammatory diseases. Moreover, due to their biocompatibility and specificity, peptides are
also becoming a focus in the development of vaccines. They can be used to mimic parts of pathogens,
thereby training the immune system to recognize and combat actual infections. This area of research is
continually evolving as we learn more about peptide design and immune interactions. Research in
regenerative medicine is also investigating peptides for their potential to promote tissue repair and
regeneration. By modulating pathways that control cell proliferation and differentiation, peptides like
LSKL-NH2 could play a role in restoring tissue structure and function, offering innovative treatments
for injuries or degenerative diseases. Thus, the potential medical applications of LSKL-NH2 are diverse,
and ongoing research is likely to expand our understanding of their full therapeutic
potential.
What are the advantages of using LSKL-NH2 in therapeutic applications?
The use of
peptides like LSKL-NH2 in therapeutic applications offers multiple advantages due to their unique
properties and versatile nature. One of the primary benefits is their specificity, which allows for
targeted interaction with biological molecules. This precision reduces the likelihood of off-target
effects and minimizes collateral damage to healthy tissues, which is a significant concern with many
conventional drugs. Specificity also translates to higher efficacy in modulating precise biological
pathways, which is vital for developing treatments that require delicate modulation of cellular
processes. Another advantage is their relatively simple synthesis and modification. Unlike larger
proteins, peptides are composed of fewer amino acids, making them easier to synthesize with precision.
This simplicity allows for extensive modifications to optimize their properties, such as stability,
solubility, and binding affinity, enhancing their therapeutic potential. Furthermore, chemical
modifications like the addition of an NH2 group can improve the half-life and bioavailability of
peptides, making them more effective in vivo. Biocompatibility and biodegradability are other
significant advantages of peptide-based therapies. They are generally well-tolerated by the body and are
broken down into amino acids, which are naturally occurring and rarely pose toxicity issues. This
profile makes them safer than many synthetic drugs or biologics that may have complex breakdown
products. This safety profile is crucial for drugs intended for long-term use or chronic conditions. The
reduced risk of immunogenicity is another benefit. Peptides are less likely to be recognized as foreign
by the immune system compared to larger molecules, reducing the risk of adverse immune reactions. This
makes them suitable candidates for chronic treatments or conditions requiring repeated dosing. Moreover,
the adaptability of peptides opens up opportunities for diverse drug delivery methods, including
topical, oral, and injectable formats, potentially improving patient compliance. Finally, peptides like
LSKL-NH2 offer opportunities for multi-targeted approaches. By designing peptides that can interact with
multiple molecular targets, researchers can tackle complex diseases where targeting a single molecule
may not suffice. This multi-target functionality can be invaluable in diseases such as cancer or
autoimmune disorders, where intricate networks of signaling pathways are involved. Ultimately, the
versatility and beneficial properties of peptides like LSKL-NH2 position them as promising candidates in
the development of next-generation therapeutics.
How is the research and development process for
a peptide like LSKL-NH2?
The research and development process for peptides, including LSKL-NH2,
involves a comprehensive series of stages designed to understand and optimize their therapeutic
potential before clinical use. The initial phase begins with identification, where researchers explore
existing literature or conduct new experimental studies to understand the peptide’s biological activity.
This phase may also involve computational modeling to predict how modifications, such as the addition of
an NH2 group, might alter its properties or interactions. After identification, synthesis and analytical
characterization are performed. Peptides can be synthesized chemically or biologically using techniques
like solid-phase peptide synthesis (SPPS), which allows precise control over the peptide sequence and
modification. Once synthesized, extensive characterization using techniques such as mass spectrometry
and NMR spectroscopy is essential to confirm the peptide's structure and purity. Preclinical studies
then commence, involving in vitro and in vivo assays to assess biological activity, potency, and
mechanism of action. These studies explore how the peptide interacts with cellular targets and
influences biological processes. Researchers also assess the pharmacokinetics and pharmacodynamics of
the peptide, studying its absorption, distribution, metabolism, and excretion (ADME) properties. This
information is critical to optimize dosing and administration routes. Toxicity and safety profiles are
evaluated through preclinical models, examining any potential adverse effects or cytotoxicity. This
stage is crucial as it determines the feasibility of moving the peptide into clinical trials. Challenges
such as stability, solubility, and potential immunogenicity are also addressed at this stage, involving
modifications to enhance the peptide's properties for therapeutic use. Upon successful preclinical
evaluation, the peptide may advance to clinical trials, where it undergoes rigorous testing in human
subjects. Clinical trials are conducted in phases, starting with phase I to assess safety and dosage in
healthy volunteers, followed by phase II and III trials to evaluate efficacy and monitor for side
effects in patients with the target condition. These trials are tightly regulated and require adherence
to ethical guidelines. Throughout this process, regulatory agencies are involved to ensure compliance
with safety and efficacy standards. Peptides like LSKL-NH2 must demonstrate a clear benefit-risk ratio
to gain approval for clinical use. The entire R&D process can be lengthy and costly, often taking
several years and requiring collaboration between interdisciplinary teams. Success relies on an
intricate understanding of biochemical interactions, disease mechanisms, and patient needs, ultimately
aiming to deliver safe and effective therapeutic solutions to the market.
How does the
biochemical structure of LSKL-NH2 influence its interaction with biological systems?
The biochemical
structure of LSKL-NH2 plays a crucial role in determining its interaction with biological systems, and
this interaction is largely contingent upon the peptide's sequence, conformation, and chemical
modifications. Peptides like LSKL-NH2 are composed of specific sequences of amino acids that determine
their three-dimensional structure and functionality. The sequence dictates how the peptide folds, which
in turn influences its ability to bind to particular cellular targets, such as receptors or enzymes. For
instance, the arrangement of hydrophobic and hydrophilic regions within the peptide can affect how it
interacts with the lipid bilayer of cell membranes or aqueous environments. The conformation of the
peptide, which is the specific three-dimensional shape it adopts, is critical in ensuring that the
active sites align perfectly with the corresponding binding sites on target molecules. This specificity
is central to the peptide's ability to modulate particular biological pathways with minimal side
effects. Modifications such as the addition of an NH2 group at the terminal end can enhance the
stability and solubility of the peptide, potentially improving its bioavailability and half-life in
biological systems. Terminal amination can also reduce degradation by exopeptidases, enzymes that target
peptide ends, thus maintaining peptide activity for longer durations within the body. Additionally, the
NH2 group may influence the peptide's charge, thereby affecting its interaction with charged biological
molecules and surfaces. The specificity of LSKL-NH2 also comes into play in its ability to engage in
hydrogen bonding, hydrophobic interactions, and van der Waals forces with target proteins, all of which
are essential for a stable and functional interaction. The overall charge, presence of functional
groups, and stereochemistry all contribute to the binding affinity and selectivity of the peptide for
its target. Environmental factors such as pH and ionic strength can further influence the interaction of
LSKL-NH2 with biological systems, as they can affect peptide stability and shape. Consequently,
understanding the biochemical structure of peptides helps researchers predict and manipulate their
biological activity for desired therapeutic outcomes. This detailed knowledge guides the design and
optimization of peptide-based therapeutics, ensuring they interact effectively within the complex milieu
of the human body to exert their intended effects.
What challenges are typically faced in the
development of peptide-based therapies like LSKL-NH2?
Developing peptide-based therapies, including
LSKL-NH2, presents a unique set of challenges that researchers and developers must address to translate
these bioactive molecules into viable therapeutic agents. One primary challenge is peptide stability.
Peptides are susceptible to rapid degradation by proteolytic enzymes in the body, which can
significantly reduce their half-life and efficacy as therapeutics. This vulnerability necessitates
chemical modifications to stabilize the peptide, such as incorporating non-natural amino acids or
terminal capping to protect against enzymatic cleavage, without compromising its specific biological
activity. Another significant challenge is bioavailability. Oral bioavailability of peptides is
particularly low due to poor absorption in the gastrointestinal tract and subsequent degradation.
Alternative routes of administration, such as intravenous, subcutaneous, or nasal delivery, may be
explored; however, each comes with its advantages and limitations in terms of patient compliance, onset
of action, and formulation requirements. Overcoming peptide immunogenicity is another critical hurdle.
While peptides are generally considered less immunogenic than proteins, the potential for invoking
immune responses still exists, particularly with repeated administration or in sensitive individuals.
Avoiding immunogenicity involves careful design, including the possible incorporation of D-amino acids
or PEGylation, a process that involves attaching polyethylene glycol (PEG) chains to increase size and
decrease recognition by the immune system. Manufacturing consistency and scalability pose additional
challenges. Producing peptides like LSKL-NH2 in a consistent and scalable manner requires advanced
technologies and stringent quality controls to ensure purity and bioactivity throughout the
manufacturing process. This need for precision can increase production costs, impacting the economic
feasibility of peptide therapeutics. Furthermore, regulatory challenges must be navigated. Peptide
therapies, like all new therapeutics, must undergo rigorous testing and evaluation to meet the safety,
efficacy, and quality standards set by regulatory bodies such as the FDA or EMA. Meeting these
requirements involves comprehensive preclinical and clinical testing to establish a favorable
benefit-risk profile, often requiring substantial time and financial investment. Despite these
challenges, advances in peptide synthesis, formulation technologies, and delivery systems continue to
push the boundaries of peptide therapeutic development. By addressing stability, bioavailability, and
immunogenicity concerns, researchers aim to harness the full therapeutic potential of peptides like
LSKL-NH2, offering innovative solutions to unmet medical needs across various disciplines.