Synonym |
FQVVC(NPys)G-amide |
Species |
Human |
Protein Accession |
NA |
Purity |
85% |
Endotoxin Level |
<1.0 EU/μg |
Biological Activity |
NA |
Expression System |
Chemical synthesis |
Fusion Tag |
NA |
Predicted Molecular Mass |
788.84 Da |
Formulation |
Supplied as a lyophilized powder |
Reconstitution |
Centrifuge vial before opening. Reconstitute in sterile ddH2O to a concentration of 1 mg/ml |
Storage & Stability |
Store at -20°C. Aliquot to avoid repeated freezing and thawing. |
FAQ
What is FQVVC(NPys)G-amide, and what are its potential applications?
FQVVC(NPys)G-amide is a
synthetic peptide that has gained attention for its potential applications in various scientific and
biomedical research areas. This peptide is composed of a specific sequence of amino acids, where the
side chain of one amino acid is modified with a pyridyl disulfide (NPys) group. This modification can
impart unique biochemical and biophysical properties to the peptide, allowing it to serve different
purposes. One potential application of FQVVC(NPys)G-amide is in drug delivery systems. The NPys group
can facilitate the formation of disulfide bonds with thiol groups present on target molecules, allowing
for stable and site-specific attachment. This feature can be particularly useful for developing targeted
drug delivery mechanisms where the peptide acts as a carrier, ensuring that therapeutic agents are
released at specific sites within the body, increasing efficacy and reducing side
effects.
Another promising field of application is in diagnostic assays and biosensing
technologies. The ability of FQVVC(NPys)G-amide to form disulfide bonds can be harnessed to immobilize
biomolecules on sensor surfaces. This facilitates the creation of sensitive and specific detection
systems for various analytes, including small molecules, proteins, and nucleic acids. The peptide's
versatility and stability under physiological conditions can enhance the performance and reliability of
diagnostic assays.
Furthermore, FQVVC(NPys)G-amide can be employed in the study of
protein-protein interactions. By incorporating this peptide into protein structures, researchers can
introduce controllable binding sites that mimic native cysteine residues, allowing detailed functional
and structural analyses. Researchers also explore applications in material science, where such peptides
can be used to modify surfaces or form supramolecular structures with advanced functions, contributing
to the development of novel materials. Overall, the unique properties of FQVVC(NPys)G-amide make it a
versatile tool with vast potential across multiple scientific fields, encouraging continued exploration
and innovation in its applications.
How does the NPys modification enhance the functionality of
FQVVC(NPys)G-amide in research settings?
The NPys modification enhances the functionality of
FQVVC(NPys)G-amide by imparting unique chemical properties that open up a wide range of applications in
research settings. The NPys group, which stands for N-pyridyl disulfide, is a reactive functional group
that allows for the formation of disulfide bonds with thiol groups. This modification is beneficial
because disulfide bonds are known for their reversible nature, which can be exploited in various
biochemical processes and manipulations.
One key advantage of the NPys modification is its role
in facilitating site-specific conjugation. In research and development, achieving site-specific
conjugation is critical in maintaining the functionality and specificity of biomolecules. The presence
of the NPys group on FQVVC(NPys)G-amide allows for targeted disulfide bond formation with free thiol
groups on other molecules, thus providing a controlled method of bioconjugation. This capability is
particularly useful in the development of targeted drug delivery systems, where the peptide can be
covalently linked to therapeutic agents, ensuring that these agents are delivered to specific cells or
tissues.
Additionally, the NPys modification provides a stable yet reversible linkage. In many
biochemical assays and applications, researchers need temporary interactions and bindings that can be
reversed or broken under specific conditions, such as a reducing environment. The disulfide bonds formed
through the NPys group can be reduced back to free thiols, enabling controlled debonding when necessary.
This reversibility is advantageous in dynamic systems and studies that require multiple cycles of
binding and release.
The NPys modification on FQVVC also enhances the peptide's utility in
biosensor development. In biosensing applications, achieving a stable and specific immobilization of
recognition elements on sensor surfaces is crucial. The NPys group can facilitate this by attaching to
thiol-modified surfaces, leading to robust and reliable sensor interfaces. This enhances the accuracy
and sensitivity of biosensors used in medical diagnostics and environmental monitoring.
Moreover,
the NPys modification can be utilized in structural biology for the strategic introduction of
site-specific modifications in proteins and peptides. Researchers can employ FQVVC(NPys)G-amide to
introduce labels or probes at precise locations in protein structures, aiding in the study of protein
folding, dynamics, and interactions without altering the protein's native structure. In summary, the
NPys modification significantly enhances the versatility and functionality of FQVVC(NPys)G-amide in
research settings, offering controlled, stable, and reversible conjugation capabilities that support
advanced scientific investigations.
What are the chemical and structural characteristics of
FQVVC(NPys)G-amide that make it suitable for biomedical applications?
The chemical and structural
characteristics of FQVVC(NPys)G-amide endow it with unique properties that make it suitable for a
multitude of biomedical applications. At its core, FQVVC(NPys)G-amide is a peptide sequence composed of
the amino acids phenylalanine (F), glutamine (Q), valine (V), valine (V), cysteine (C), glycine (G), and
amide at the C-terminus, with a pyridyl disulfide (NPys) modification on the cysteine. This specific
sequence and chemical modification offer distinct advantages in terms of stability, reactivity, and
biofunctionality.
Firstly, the presence of the NPys modification is critical for the peptide's
application in bioconjugation and targeted delivery systems. The NPys group introduces reactive
disulfide chemistry, allowing FQVVC(NPys)G-amide to form covalent disulfide linkages with free thiol
groups on other molecules. This is a significant advantage in designing drug delivery systems where the
peptide can act as a carrier, ensuring the specific attachment and release of therapeutic agents at
targeted sites within the body. These capabilities are particularly sought after in precision medicine,
where targeting specific cells or tissues while minimizing off-target effects is
essential.
Structurally, the peptide backbone confers stability and adaptability in physiological
conditions. The specific sequence of amino acids is engineered to offer stability in various
environments, including the presence of enzymatic activity, which is crucial for systemic circulation in
vivo. This stability ensures that the peptide remains intact until it reaches its desired target site,
thereby protecting the payload and reducing degradation before delivery.
Furthermore, the
peptide's relatively small size compared to larger protein counterparts offers several benefits. The
smaller size can facilitate better penetration into tissues and cells, enhancing its ability to reach
and interact with intracellular targets. In diagnostic applications, this can lead to improved
sensitivity and specificity, as the peptide can be conjugated with signal molecules to increase
detection capabilities.
The amide termination at the C-terminus offers additional stability
against proteolytic degradation, a common challenge in peptide-based therapeutics and diagnostics. Amide
groups can enhance the overall chemical stability of peptides, ensuring that they retain their integrity
and functional properties throughout their intended application.
In addition to these properties,
the inherent flexibility of peptide chemistry allows for further modifications and customizations, which
can be tailored to specific biomedical applications. Researchers can design derivatives of
FQVVC(NPys)G-amide to incorporate additional functional groups, labels, or ligands, thereby broadening
its application range from drug delivery and diagnostics to therapeutic treatments and beyond. In
summary, the combination of the NPys modification with the peptide's inherent structural and chemical
properties makes FQVVC(NPys)G-amide a versatile and valuable tool in the realm of biomedical
applications.
Can FQVVC(NPys)G-amide be used in targeted drug delivery systems, and how does it
contribute to precision medicine?
FQVVC(NPys)G-amide holds significant potential for use in
targeted drug delivery systems, a cornerstone technology in precision medicine. The peptide's unique
properties, particularly the presence of the NPys modification, provide several mechanisms to enhance
targeted delivery strategies, contributing significantly to precision medicine's goal of delivering the
right therapeutic interventions to the right patients at the right time.
In targeted drug
delivery systems, FQVVC(NPys)G-amide can serve as a versatile linker or carrier for therapeutic
molecules. The NPys modification enables the peptide to form covalent disulfide bonds with thiol groups
on other molecules, such as drugs, antibodies, or ligands. This functionality facilitates the
site-specific attachment of therapeutic agents to the peptide, which is critical for ensuring that drugs
are delivered precisely to their intended sites of action. This specificity can significantly enhance
the therapeutic index of drugs, maximizing efficacy while minimizing side effects. For instance, in
cancer treatment, targeted delivery can concentrate anti-cancer drugs directly to tumor cells, sparing
healthy tissues and reducing systemic toxicity.
Moreover, the disulfide bonds formed via the NPys
group can be designed to be cleavable under certain physiological conditions, such as the reducing
environment within cells. This property allows for controlled release of the therapeutic payload once
the peptide-drug conjugate reaches the target site. Controlled release is a vital feature in precision
medicine, ensuring that drugs exert their action precisely where needed, over a sustained period, and at
optimal concentrations. Such controlled release mechanisms enhance the precision and efficiency of
treatment regimens, offering a higher probability of therapeutic success.
FQVVC(NPys)G-amide also
contributes to the development of multifunctional drug delivery platforms. These platforms can carry
multiple therapeutic agents or combine therapeutic and diagnostic functions (theranostics), making it
easier to tailor treatments to individual patient needs based on comprehensive diagnostic information.
Personalized treatment regimens based on such multifunctional systems align well with the principles of
precision medicine.
Additionally, the peptide's small size and stability make it advantageous for
use in a range of delivery modalities, including nanoparticles, liposomes, and micelles. These delivery
vehicles can be engineered to leverage the protective and targeting capabilities of FQVVC(NPys)G-amide,
improving their pharmacokinetic and biodistribution profiles.
In summary, FQVVC(NPys)G-amide
enhances targeted drug delivery through its site-specific conjugation capability, controlled release
potential, and versatility in delivery system integration. These features collectively support the
advancement of precision medicine by enabling more targeted, effective, and personalized therapeutic
interventions. Through its application in targeted drug delivery, FQVVC(NPys)G-amide can help to fulfill
the promise of precision medicine, offering hope for treatments that are both highly effective and
tailored to individual patient contexts.
How can FQVVC(NPys)G-amide be utilized in the
development of biosensors, and what advantages does it offer in biosensing
applications?
FQVVC(NPys)G-amide presents a compelling component in the development of biosensors
due to its unique chemical properties, notably the NPys group, which provides versatile and stable
immobilization capabilities crucial for biosensing applications. Biosensors are analytical devices that
convert a biological response into a quantifiable signal, and the efficiency, sensitivity, and
specificity of these devices heavily depend on the effective integration of biological and electronic
components. FQVVC(NPys)G-amide can significantly enhance these attributes, making it a valuable tool in
the biosensing field.
The NPys modification on the peptide enables it to form stable disulfide
bonds with thiol groups, which is particularly useful for the immobilization of biomolecules onto
biosensor surfaces. This site-specific and robust attachment is critical in maintaining the activity and
orientation of biological recognition elements like enzymes, antibodies, or DNA aptamers on sensor
platforms. Proper orientation is essential for ensuring maximum bioactivity and sensor response, which
directly affects the sensitivity and reliability of the biosensor.
Additionally, the reversible
nature of disulfide bonds provides a mechanism for regenerating the sensor surface by facilitating the
controlled removal and replacement of bioactive elements. This regenerability is advantageous for
creating reusable biosensors, reducing costs, and extending sensor longevity. In environments where
biosensors face fouling or degradation, this capability can prove critical, as it allows for easy
restoration of sensor functionality.
Moreover, the incorporation of FQVVC(NPys)G-amide can
enhance the specificity of biosensors. The peptide's sequence can be modified or conjugated with
specific ligands that preferentially bind to target analytes. This customization is vital for designing
biosensors that are selective for particular molecules or pathogens, such as specific biomarkers in
medical diagnostics or toxic chemicals in environmental monitoring.
In practical applications,
FQVVC(NPys)G-amide can be integrated into various sensing platforms, including electrochemical, optical,
and piezoelectric biosensors. Its stability and reactivity are compatible with differing transducer
requirements, allowing it to enhance signal fidelity and transduction efficiency. For example, in
electrochemical biosensors, the peptide can improve electron transfer between the sensor surface and
biological recognition elements, resulting in more accurate and rapid detection.
In optical
sensors, FQVVC(NPys)G-amide can be used to strategically position fluorescent or plasmonic labels,
boosting signal intensity and providing real-time analysis capabilities. This versatility and
adaptability to different sensing environments and technologies make it an attractive option for
developing next-generation biosensors with improved performance and broader application
capabilities.
In conclusion, FQVVC(NPys)G-amide’s ability to provide stable and specific
immobilization of biological recognition elements, its potential for regenerable sensor surfaces, and
its adaptability to various sensing technologies greatly enhance biosensor performance. These properties
contribute to advanced biosensing applications that demand high sensitivity, specificity, and
reliability, thus supporting ongoing innovation and advancement in the field of biosensing technology.