Peptide Scanning
Peptide Scanning - Related Videos
08:09
Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
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Cited by 15 •
2017
Here, the authors present a simple and efficient protocol to define a linear antigenic epitope using a purified monoclonal antibody and peptide scanning through dot-blot hybridization. The identified epitope can then be used in therapeutic and diagnostic applications.
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.
02:28
Leaky Scanning
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2020
During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
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.
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.
FAQs
Researchers compare a reference peptide with targeted variants that alter individual residues or sequence segments. A change in antibody, receptor, enzyme, or other biomolecular interaction shows that the modified position contributes to recognition, binding, or activity. Comparing these effects across variants helps distinguish sequence features that are essential from those with smaller functional influence.
Overlapping peptides share portions of the original sequence while shifting the tested region along the peptide. If neighboring peptides produce similar interactions, the shared sequence may contain a relevant binding or recognition feature. This arrangement helps narrow the location of antigenic epitopes, binding motifs, or functional regions without relying on a single peptide sequence.
Variant-to-variant differences can show whether a sequence change affects interaction strength, recognition, or another measured activity. Testing peptides against antibodies, receptors, enzymes, or other biomolecules connects a particular sequence feature with an observable outcome. The resulting pattern can clarify which regions support molecular contact and which changes alter biological behavior.
A typical workflow begins by selecting a reference peptide and designing overlapping peptides, targeted variants, or both. The resulting series is tested under controlled assay conditions against the relevant antibody, receptor, enzyme, or other biomolecule. Researchers then compare the measured interactions or cellular outcomes across sequences to map important residues and regions.
In immunology, the method can help map antigenic epitopes, which are peptide regions recognized by antibodies or involved in immune-related molecular interactions. Testing overlapping sequences allows researchers to associate recognition with narrower sequence segments. This information supports studies of antigen recognition and can guide investigation of how sequence changes affect antibody interactions.
Drug discovery studies can use sequence comparisons to identify peptide regions associated with binding or activity, while therapeutic optimization examines how targeted changes alter measurable molecular or cellular outcomes. These results help connect sequence design with biological performance. The approach therefore supports refinement of peptide candidates and investigation of protein interactions relevant to potential therapies.