Biotin Labeled Peptides

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 Peptide

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)

Peptide Biotinylation Services

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-labeled of Peptide Fragments

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.

• Biotin-labeled Signal Peptides

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.

• Biotin-labeled Drug Delivery Peptides

The introduction of biotin labeling into drug delivery peptides can achieve targeted delivery and release of drugs, and improve drug efficacy and selectivity.

Biotin Peptide Synthesis

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:

• Protective group selection: Before starting the peptide chain synthesis, an appropriate protective group needs to be selected to protect the amino acid residues that are not to be reacted.
• Biotin labeling group introduction: Biotin molecules are introduced at specific positions in the synthesized peptide chain. This can be achieved by chemically reacting reagents such as biotin-NHS esters or biotin-diimide with the side chains of amino acid residues. These reagents have reactive biotin moieties that can react with specific functional groups on the amino acid residues to form covalent bonding connections.
• Peptide chain synthesis: Using solid-phase synthesis techniques, the peptide chain length is gradually expanded by sequential addition of protective group removal, coupling of amino acid monomers, and washing steps according to the designed peptide sequence.
• Deprotection and purification: After synthesizing the complete peptide chain, it is necessary to remove the protecting groups and purify the target peptide. Pure biotinylated peptides are usually obtained using appropriate deprotection reagents and purification techniques.
• Validation of biotinylated peptides: Validation can be done by mass spectrometry, SDS-PAGE gel electrophoresis and other techniques to confirm the presence and purity of the labeled peptide fragments.

Application of Biotinylated Peptide

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.

Our Advantages

• A rapid and high flux platform for peptide synthesis
• Strict quality control: MS and HPLC identification results are provided for each peptide product
• Optimized Chemistries: Expertise in hundreds of cross linking modifications, activation and/or conjugation with reactive cross linkers with optimized labeling ratio
• Superior technical support: assist client from design to delivery

Project Workflow

Reference

1. Matsumura S, et al. Construction of biotinylated peptide nanotubes for arranging proteins[J]. Molecular BioSystems, 2005, 1(2): 146-148.