Biotinylation of peptides is an efficient method for conjugating specific peptides to streptavidin-coated surfaces. Due to the high affinity and binding specificity of biotin, the biotinylation interaction (biotin-avidin or biotin-streptavidin) is used as the basis of laboratory research techniques for labeling, detecting, and purifying peptides. CD Formulation offers a wide range of peptide biotinylation services to meet your diverse research needs.
Biotinylation is the process of incorporating biotin groups or residues into biomolecules such as peptides, proteins, and other macromolecules. For decades, the biotin-streptavidin interaction has been used as the basis for other labeling techniques for labeling, detection, and purification of peptides, proteins, and other biomolecules due to its specificity and high affinity (Kd < 10 - 10 M). Biotinylation of peptides is a very successful and efficient method for binding peptides to streptavidin-coated surfaces and is frequently used to label peptides. Biotinylated peptides have the following properties:
Fig. 1 Methods of selective biotinylation. (Dundas CM, et al., 2013)
As experts in peptide modification, CD Formulation provides unrivaled peptide biotinylation services to clients worldwide. With our robust synthesis procedures and superior peptide analysis technologies, we can address any possible challenge in the development and production of peptide therapeutics.
In our peptide synthesis laboratory, biotinylation labeling is typically performed at the end of the polypeptide chain but can be located anywhere along the chain. Biotinylation of the N-terminus or amino terminus occurs directly on the primary terminal amino group (-NH 2 ), while biotinylation of the C-terminus or carboxyl terminus occurs on the ε-amino group of the (extra) C-terminal lysine.
Our team of peptide modification experts can synthesize peptides using a range of biotin tags as well as custom peptide synthesis using a range of other tags.
Biotin N-Terminal Labeling | Biotin (Lysine ) C-Terminal Labeling | Biotin (EDA) C-Terminal Labeling |
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The key consideration for peptide biotinylation is to have enough spacer between the biotin group and the amino acid to ensure the desired interaction between the peptide and the macromolecule. Adding a spacer or linker between biotin and the peptide can effectively reduce the steric hindrance during the subsequent binding process. We offer a variety of spacers and linkers to meet specific needs.
Aminocaproic Acid
PEG-Spacer
The biotin-avidin or streptavidin interaction is essentially irreversible under physiological conditions. Biotin binding is resistant to pH or temperature changes, organic solvents, and denaturing agents. Therefore, we will use the following biotin analogs if you need a reversible interaction.
Iminobiotin is an analog of biotin that can be used in cases where the avidin (streptavidin)-biotin complex is slightly dissociated. This is mainly due to the replacement of its upper ring structure with a 2-imino imidazole structure, which leads to a weakened interaction with the avidin or streptavidin binding site.
Desthiobiotin is a sulfur-free biotin analog with the advantages of a high level of specificity and is not easily oxidized. It doesn't bind as tightly to avidin and streptavidin as biotin.
In addition to peptide synthesis capabilities, CD Formulation combines flexible GMP manufacturing facilities with cutting-edge peptide analytical knowledge to provide a full range of quality control testing services to accelerate the commercialization of your products, including:
Published Data
Technology: Biotinylated Peptide Synthesis
Journal: Mol Biosyst.
IF: 3.137
Published: 2005
Results:
The authors designed and synthesized three biotinylated peptides with different linkers between biotin and b-sheet peptides, and used these biotinylated designed peptides to modify 100-nanometer-sized peptide fibers. Characterization was performed using transmission electron microscopy. The results showed that the biotinylated peptides self-assembled in aqueous solution to form tubular structures with an outer diameter of about 60 nm and an inner diameter of about 30 nm. The structures of the three biotinylated peptides are shown in the figure below, which consist of three parts, including biotin, linker, and b-sheet forming region FI.
Fig. 2 The structures of the designed biotinylated peptides. (Matsumura S, et al., 2005)
CD Formulation has extensive experience with each biotin modification of peptides. Please don't hesitate to contact us if you are interested in our services, and to learn more about the possibilities of incorporating biotin into your peptides. We look forward to cooperating with you.
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