Based on our team of highly trained biological and organic chemists, BOC Sciences can provide chemical cross-linking services to our customers to precisely fit your requirements. As a full-service support partner or as a research partner, we are able to satisfy clients' needs.
Crosslinking agents are widely used to modify nucleic acids, drugs and polymers. The same principle applies to protein modification/labeling. Depending on factors such as spacer group length, there are different types of crosslinking reagents, each with a specific function and application. In particular, bifunctional small molecules with highly selective reactivity are introduced into protein-protein crosslinking and are able to specifically immobilize amines, thiols, and other functional groups.
Fig.1 The crosslinking procedures. (Li et al., 2023)
The primary focus of BOC Sciences' services is to support consistent, high-quality protein /peptide crosslinking and to apply them to different research projects. We provide research solutions based on the individual needs of our clients.
| Chemical Crosslinking | Specification |
| Disulfide Crosslinking | Disulfide crosslinking is a chemical process that involves the formation of a covalent bond between two thiol (-SH) groups, resulting in the formation of a disulfide bond (-S-S-). The efficiency and specificity of disulfide crosslinking can be affected by factors such as pH, temperature, and the presence of reducing or oxidizing agents. Therefore, the reaction conditions must be carefully optimized to achieve the desired cross-linking results. |
| Azide Crosslinking | Azide crosslinking utilizes the reaction of azide groups with specific functional groups introduced in proteins, which results in the modification of the protein. Azide crosslinking has some advantages in protein/peptide crosslinking, such as high reaction selectivity, high crosslinking efficiency, and compatibility with biological systems. |
| Polyethylene Glycol (PEG) Crosslinking | The activated proteins/peptides are combined with functionalized PEG molecules, resulting in the covalent binding of the reactive functional groups. The PEG molecules act as bridges to link the protein/peptide chains together to form a three-dimensional crosslinked network. The degree of cross-linking is controlled by adjusting the concentration of PEG, reaction time, temperature, and the presence of a catalyst or initiator. |
Chemical cross-linking can enhance the stability of proteins or other biomolecules. By forming covalent or other strong bonds, cross-linking can make proteins structurally stronger and resistant to denaturation, degradation, or dissociation.
Chemical cross-linking can be used to control and regulate the structure of proteins, peptides, or other biomolecules. By choosing different cross-linking reagents, reaction conditions, and cross-linking sites, cross-links can be introduced at specific locations to alter the conformation and function of the molecule.
Chemical cross-linking allows the joining of different types of molecules to enable the construction of multifunctional complexes or materials. This versatility makes crosslinked molecules promising for a wide range of applications such as drug delivery, biomaterial design and biosensors.
The reversibility of chemical cross-linking makes cross-linked molecules more flexible in situations where modulation or modification is required. By adjusting the reaction conditions, such as changing the temperature, and pH or adding a reducing agent, the crosslinked molecules can be dissociated and the original molecular structure can be restored.
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