BOC Sciences is committed to providing the biotechnology industry with the most complete biotinylation development services. We have extensive expertise in biotinylation, various antibodies, peptides and splicing technologies. We can provide one-stop service to maximize support for the development and manufacture of biotinylated peptides. Meanwhile, we have a quality assurance system and experimental validation process to ensure the quality and reliability of the biotinylated peptides we provide.
Biotinylated peptides are compounds in which biotin is covalently bound to a polypeptide chain. Polypeptides are short chains of proteins linked by multiple amino acid residues, whereas biotin is a small organic molecule with a high affinity and specificity for binding to pro-biotin proteins. By labeling biotin onto a peptide chain, biotin-prophilic biotin interactions can be exploited for a variety of applications such as detection, purification and visualization.
Fig.1 The structures of the designed biotinylated peptides. (Matsumura et al., 2005)
BOC Sciences has developed a wide range of services for the covalent attachment of various types of peptides to biotin. With expertise in bioconjugation, we offer tailor-made biotin-labeled peptide services to institutional and industrial customers.
Biotin can label specific peptide fragments, which may be functional regions of proteins, recognition sites, or signal sequences, among others. Labeling these peptide fragments can be used to study their biological activity, interaction partners, and localization in the cell.
Signal peptides are a class of short peptide sequences used for signaling and communication between cells. Biotin labeling can help study the biological activity, receptor binding affinity and signaling pathways of signal peptides.
The introduction of biotin labeling into drug delivery peptides can achieve targeted delivery and release of drugs, and improve drug efficacy and selectivity.
Peptide biotinylation can be carried out either at the N-terminus or the C-terminus. N-terminal biotinylation can be carried out directly on the primary terminal amino group, while biotinylation is usually carried out on the ε-amino group of the C-terminal lysine. An important consideration in the preparation of biotinylated peptides is to ensure that there are sufficient spacer arms between the biotin moiety and the amino acids in the peptide that are expected to interact with the macromolecule.
Biotinylated peptide synthesis is usually carried out using solid-phase synthesis techniques, and the following are the general steps of the method:
Biotin labeled peptides can be used for protein purification, detection, curing, drug targeting, protein structure analysis and so on. The simplest way to detect a substance that interacts with a polypeptide is to use the peptide to do affinity pull-down experiments, and then directly detect the binding protein. Protein in vitro binding (Pull-down) test can be used to verify the existence of protein-protein interactions (predicted by other methods, such as immunoprecipitation) and as a primary screening test to identify unknown protein-protein interactions. By competitive blocking binding, synthetic peptides are often used to verify hypothetical protein-protein interactions.
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