Biotin-Peptide g is a highly flexible and cell penetrating peptide that has the capability to perform a variety of biological functions. It has many important applications in biotechnology. In addition to its ability to function as a flexible base for designing infectious multi-drug resistant bacteria, it can also be used as a cost-effective base for biomedical screening assays.
Biotin-Peptide g accumulated on the plasma membrane of A549 cells within a few minutes. When labeled with anti-CD98 antibody, it partially colocalized with CD98. The resulting overlay image reveals colocalization of Biotin-Peptide g with mito-APEX2.
Peptide-level enrichment was conducted to increase the specificity of the biotinylation process. The number of detected peptides was subsequently filtered and autovalidated using protein-polishing autovalidation. This filtering system allowed the identification of 4,810 distinct biotinylated peptides from 1:50 biotin peptide to nonbiotin peptide spike-in samples.
Several factors affect the solubility of a peptide. These include the position of the biotin moiety and the spacer group. For instance, the position of the peptide’s N-terminus has a dramatic effect on the solubility of the peptide. Hence, a hydrophilic PEG chain can be used to improve the solubility of the peptide biotin conjugate.
However, proximity studies do not capture the dynamic folding states of proteins. Thus, a shorter labelling time may not be sufficient to capture the full fold. Moreover, the high concentrations of activated biotin may lead to saturation of less accessible folded regions. Therefore, a more sensitive assay is needed.