D-peptide Imaging
D-peptide Imaging - Related Videos
06:54
MR Molecular Imaging of Prostate Cancer with a Small Molecular CLT1 Peptide Targeted Contrast Agent
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Cited by 3 •
2013
To demonstrate MR cancer molecular imaging with a small peptide targeted MRI contrast agent specific to clotted plasma proteins in tumor stroma in a mouse prostate cancer model.
04:00
Immunoaffinity Based Extraction of Ubiquitinylated Peptides: A Technique to Selectively Extract Ubiquitin Tagged Peptides from Purified Peptide Fractions
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2023
This video describes a method to extract and purify ubiquitinylated peptides containing remnant di-glycine peptides from a complex peptide mixture. The presented method may help in identifying original ubiquitination sites in the protein.
07:03
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Cited by 18 •
2014
This procedure demonstrates in vivo near IR fluorescence imaging of collagen remodeling activities in mice as well as ex vivo staining of collagens in tissue sections using caged collagen mimetic peptides that can be photo-triggered to hybridize with denatured collagen strands.
12:27
Measuring Peptide Translocation into Large Unilamellar Vesicles
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Cited by 9 •
2012
This protocol details a method for the quantitative measure of peptide translocation into large unilamellar lipid vesicles. This method also provides information about the rate of membrane translocation and can be used to identify peptides that efficiently and spontaneously cross lipid bilayers.
07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Cited by 6 •
2013
This paper describes the formation of highly ordered peptide-based structures by the spontaneous process of self-assembly. The method utilizes commercially available peptides and common lab equipment. This technique can be applied to a large variety of peptides and may lead to the discovery of new peptide-based assemblies.
FAQs
The mirror-image configuration can make these peptides resistant to degradation by many proteases, which are enzymes that break down peptide chains. Greater resistance may allow a probe to remain available long enough to interact with its biological target and carry its imaging signal. This persistence supports visualization of disease-associated molecules in living systems, including those associated with tumors.
Selective recognition determines whether a probe can distinguish a disease-associated molecule from unrelated biological components. When a D-peptide binds a relevant target, its attached signal can provide information about the target’s location and distribution. In cancer research, this property supports molecular characterization of tumors rather than relying only on their physical appearance.
Protease resistance helps preserve the imaging probe after it enters a living system. Because many proteases can degrade ordinary peptide structures, resistance may extend the time available for target binding and signal detection. This characteristic is especially relevant when researchers need to visualize tumor-associated targets or follow changes during cancer treatment.
A probe is designed around a D-amino-acid peptide that can recognize a selected biological target, then paired with an imaging agent suited to the intended modality. The resulting construct is used to visualize target-associated signals in living systems. Probe design therefore connects molecular recognition with the type of signal required for detection or study.
The source describes radioactive, fluorescent, and magnetic resonance-compatible labels as possible signal-producing components. Each option supports a different imaging approach, while the D-peptide supplies target-directed recognition and stability. Selecting among these label types allows researchers to align the probe with the imaging system used to examine tumors or other disease-associated biological targets.
Cancer researchers can use these probes for tumor detection, molecular characterization, treatment planning, and monitoring therapeutic response. The approach can reveal where selected disease-associated molecules occur and help track changes relevant to tumor biology. These applications make D-peptide imaging useful for developing noninvasive diagnostics and for studying how tumors behave during therapy.