Peptide Functionalization
Peptide Functionalization - Related Videos
14:28
Peptide-based Identification of Functional Motifs and their Binding Partners
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Cited by 2 •
2013
Techniques to dissect the mechanisms underlying the secretion of HIV-1 Nef in exosomes are described. Specific short peptides derived from Nef and protein transfection were exploited to determine the structure, function, and binding partners of Nef’s Secretion Modification Region. These procedures have general relevance in many mechanistic studies.
11:42
Solid Phase Synthesis of a Functionalized Bis-Peptide Using "Safety Catch" Methodology
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Cited by 2 •
2012
The efficient solid-phase peptide synthesis of a functionalized bis-peptide trimer utilizing a "safety catch" cleavage procedure from HMBA resin is described.
15:33
Microwave-assisted Functionalization of Poly(ethylene glycol) and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
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Cited by 32 •
2013
This video will illustrate a rapid, efficient method to methacrylate poly(ethylene glycol), enabling chain polymerizations and hydrogel synthesis. It will demonstrate how to similarly introduce methacrylamide functionalities into peptides, detail common analytical methods to assess functionalization efficiency, provide suggestions for troubleshooting and advanced modifications, and demonstrate typical hydrogel characterization techniques.
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.
06:45
Quantifying the Antifungal Activity of Peptides Against Candida albicans
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Cited by 5 •
2023
This protocol describes a method for obtaining quantitative data on the antifungal activity of peptides and other compounds, such as small-molecule antifungal agents, against Candida albicans. Its use of optical density rather than counting colony-forming units to quantify growth inhibition saves time and resources.
FAQs
Selective coupling targets particular reactive groups at peptide termini or on amino acid side chains. Amines, thiols, and carboxylates can serve as attachment points for labels, lipids, polymers, or other molecular components. Controlling which group reacts helps researchers introduce a desired function while limiting unintended changes elsewhere in the peptide.
Protecting groups temporarily mask reactive termini or side chains so they do not participate in an unwanted coupling reaction. This control is especially useful when a peptide contains multiple amines, thiols, or carboxylates. After the intended attachment is formed, the protection strategy can be removed or adjusted to preserve the peptide’s planned functional pattern.
The selected attachment site determines how an added label, lipid, polymer, or other component is positioned relative to the peptide. Modifying a terminus differs from modifying an amino acid side chain because each location can alter how the peptide is examined or used. Site choice therefore supports goals such as labeling, immobilization, stability, or activity control.
Functional groups can connect peptides to fluorescent labels, lipids, polymers, or other molecular components, giving the resulting construct properties that the unmodified peptide lacks. These additions may support detection, surface attachment, delivery, or improved stability or activity. The intended application determines which component and coupling site are most useful for the design.
A typical workflow begins by selecting the peptide terminus or side chain and the molecular component to be attached. Researchers then choose a compatible reactive group, apply protecting groups when needed, and carry out the coupling under controlled conditions. The resulting functionalized peptide is used for the planned biochemical investigation or application, such as labeling or immobilization.
Researchers can functionalize peptides when they need to track them with fluorescence, attach them to a surface, or connect them to another molecular component. These modifications help investigate peptide structure and interactions while providing a defined handle for experimental use. The same strategy can support biosensor and diagnostic development when peptide recognition or detection is required.
In therapeutic design, attaching selected molecular components can help explore changes in peptide stability, activity, or delivery. Lipids and polymers are among the components used for this purpose, while other modifications can support investigation of peptide behavior. Functionalized constructs therefore connect chemical modification with the development of peptide-based therapeutics and drug-delivery approaches.