Synonym |
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 |
Species |
Human |
Protein Accession |
Unknown |
Purity |
95% |
Endotoxin Level |
<1 EU/μg |
Biological Activity |
Not specified |
Expression System |
Chemical synthesis |
Fusion Tag |
None |
Predicted Molecular Mass |
1054.2 Da |
Formulation |
Lyophilized powder |
Reconstitution |
Reconstitute in water to a concentration of 1 mg/ml |
Storage & Stability |
Store at -20°C upon receipt, stable for up to 6 months at -80°C |
FAQ
What is Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 and what are its primary applications in research
and development?
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 is a highly specialized peptide
designed for use in various types of biochemical and physiological research. This sophisticated compound
is utilized primarily in the study of enzyme-substrate interactions, protein-protein interactions, and
cell signaling pathways. Researchers employ this peptide due to its unique properties that allow for
examination of complex biological processes in systems where traditional methods may not be effective.
In particular, this peptide is used in assays aimed at understanding the structure and function of
specific proteins and enzymes, which are vital for numerous biological activities. Its design
incorporates particular amino acid sequences that mimic parts of proteins or enzymes that are of
interest in these studies. Moreover, Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 is embedded with
chromogenic or fluorogenic groups that are used to produce signals when certain biological events occur,
serving as a means of detection in biochemical assays. It is also engineered to incorporate specific
modifications that enable it to act as an inhibitor or activator, providing an effective tool for
modulating certain biochemical pathways in research settings. This peptide serves a crucial role in
experimental research directed at drug discovery and design, as understanding the detailed interactions
at the molecular level can guide the development of therapeutic agents. By providing insight into the
biological functions of proteins and enzymes, it assists researchers in elucidating the mechanisms
underlying various diseases and identifying potential targets for pharmaceutical intervention.
Furthermore, in clinical diagnostics and therapeutic research, this peptide aids in identifying
biomarkers and assessing the efficacy of novel drugs. It aligns perfectly with the needs of cutting-edge
research, offering an invaluable resource for scientists dedicated to advancing the frontiers of
biochemistry and molecular biology.
How does the structural composition of
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 enhance its functionality in biochemical
research?
The structural composition of Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 is
meticulously designed to enhance its functionality in biochemical research, boasting features that
interact optimally with biological macromolecules. The sequence of amino acids is carefully chosen to
mimic natural peptides yet includes innovative modifications that improve its stability, activity, and
specificity. One of the standout features of this peptide is the inclusion of the fluorescent group Mca,
a derivative of 7-methoxycoumarin, which emits a fluorescent signal upon hydrolysis or interaction with
specific biochemical targets. This characteristic allows the peptide to be used in fluorescence-based
assays, providing a detectable readout of biochemical interactions in real-time and enabling researchers
to monitor enzyme activities or protein interactions dynamically. Additionally, the presence of unique
amino acids such as β-cyclohexyl, AG, Nva, and HA contribute to diverse interactions with proteins and
enzymes, enhancing binding specificity and affinity. This precise arrangement allows for the exploration
of enzyme kinetics and the detailed investigation of enzymatic pathways. Another pivotal component, the
Dap(Dnp) group, acts as a quenching element that interacts with the fluorescent moiety. When the peptide
is intact, this quenching effect minimizes background signal; however, upon cleavage or significant
interaction, the quenching is lifted, resulting in a quantifiable fluorescence increase. This property
is particularly valuable in enzymology studies, where activity-dependent changes are crucial for
analysis. Moreover, these elements confer resistance to proteolytic degradation, boosting its durability
in experimental setups, especially where extended assays are required or under conditions mimicking
physiological environments. The terminus NH2 end enhances cellular uptake and facilitates penetration
across biological membranes, which is essential for in vivo and in vitro studies requiring intracellular
activity observation. Through these multidisciplinary attributes embedded within its structure,
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 stands out as an exceptional tool in the arsenal of
biochemical research methodologies.
What are the benefits of using
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 over traditional biochemical assay
reagents?
Utilizing Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 in biochemical assays provides
numerous benefits over traditional reagents, primarily due to its advanced design tailored for high
sensitivity and specificity. One of the primary advantages is its ability to provide real-time analysis
through fluorescence-based detection. Traditional biochemical assays often rely on colorimetric or
endpoint measurements, which can be limited by their resolution and sensitivity. In contrast, this
peptide incorporates a dynamic fluorescent signal that permits continuous monitoring of enzymatic
activities and protein interactions with high temporal precision, enabling the capture of transient or
rapid biochemical events that might be missed by slower methods. Besides its dynamic range, the
specificity offered by Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 is significant. It is engineered for
selective interaction with designated enzymes or proteins, leading to greater accuracy and less
interference from off-target activities. This selectivity is crucial in complex biological matrices
where multiple chemical processes occur simultaneously. Traditional reagents may lack this level of
specificity, resulting in background noise that can obscure true signals or necessitate more extensive
purification steps. Additionally, this peptide is valuable due to its stability, a feature that is not
always present in standard biochemical reagents that can degrade over time or under experimental
conditions. Its resistance to proteolytic degradation and environmental factors ensures consistent
performance throughout the duration of experiments, allowing researchers to extend the time frame of
assays without the risk of reagent breakdown affecting results. Another key advantage lies in its
versatility; the peptide can be modified or tailored for specific research needs, such as including
additional functional groups or isotopic labels to facilitate a broader range of assay types. This
adaptability is less feasible with traditional reagents, which tend to have fixed functionalities. These
benefits collectively make Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 a superior choice over
conventional assay reagents, catering to the nuances and demands of cutting-edge biochemical
research.
Could you describe some of the recent research breakthroughs facilitated by using
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2?
Recent research leveraging
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 has resulted in significant breakthroughs across various
domains of biochemistry and molecular biology, underscoring its value as a research tool. A notable
example includes advancements in understanding enzyme mechanisms, particularly those involved in human
diseases such as cancer and neurodegenerative disorders. By employing this peptide, researchers have
been able to unravel the kinetics of enzyme inhibition, providing insights into potential drug targets.
The real-time fluorescent assays facilitated by this peptide have allowed for precise mapping of enzyme
activities and the identification of critical sites for therapeutic intervention. In cancer research,
specifically, the ability to evaluate protease activity within living cells has been enhanced, leading
to discoveries about the role of these enzymes in tumor progression and metastasis. This peptide's
sensitivity and specificity have enabled scientists to observe the inhibition of proteolytic enzymes by
candidate drugs in real-time, paving the way for developing more effective treatments. In neurobiology,
the structural motif offered by Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 has helped delineate
amyloid-beta peptide interactions implicated in Alzheimer's disease pathology. Researchers have utilized
the fluorescence capabilities to directly observe aggregation processes and test compounds that might
disrupt harmful protein interactions. In the realm of infectious diseases, the peptide has contributed
to breakthroughs in understanding pathogen enzyme systems responsible for bacterial virulence. By
accurately measuring the activity of these enzymes under different conditions or in response to
potential antibiotics, it has guided the design of new antimicrobial strategies. Moreover, its
utilization in studying cell signaling pathways has expanded knowledge regarding immunological
responses, illustrating how specific interactions modulate immune system functions and offering targets
for modulating immune-related disorders. Across these varied fields,
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 continues to be an instrumental tool, driving forward
research efforts with its unparalleled precision and utility in complex biological
investigations.
What challenges can researchers encounter when using
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2, and how can they be overcome?
Despite its numerous
advantages, researchers may encounter a few challenges when using
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2, though these can be effectively managed with careful
experimental design. One potential challenge is the optimization of assay conditions to ensure accurate
and reproducible results. Given its sensitivity, the peptide requires precise control over assay
parameters such as pH, temperature, and ionic strength to function optimally. Variations in these
conditions could affect the stability of the peptide or the fluorescence signals, leading to variability
in measurements. Researchers can overcome this by conducting thorough preliminary experiments to
optimize conditions specific to their system and ensuring consistent assay environments with calibrated
equipment. Another challenge involves interference from other fluorescent sources present in complex
biological samples. This can potentially mask or alter the fluorescence signal generated by the peptide.
To mitigate this issue, researchers should employ appropriate controls and spectral analysis techniques
to differentiate signal contributions from the peptide and background components. Employing fluorescence
filters and detectors optimized for the specific wavelengths emitted by the peptide can help enhance the
signal-to-noise ratio. Moreover, interpreting results from fluorescence-based assays often requires
specialized knowledge and data analysis competencies. The multivariate nature of data gathered using
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 necessitates robust statistical methods to derive accurate
conclusions. Researchers can prepare for this by gaining proficiency in relevant data analysis software
and techniques, such as those pertaining to kinetic analysis or image processing. Finally, while the
peptide is designed for resistance to degradation, long-term storage and handling must be managed
carefully to prevent issues. Maintaining appropriate storage conditions, such as refrigeration and
protection from light, will help preserve its integrity over time. Through strategic planning and the
application of rigorous scientific methodologies, the challenges associated with using
Mca-Pro-β-cyclohexyl-AG-Nva-HA-Dap(Dnp)-NH2 can be surmounted, allowing researchers to harness the full
potential of this innovative research tool in advancing scientific discovery.