A peptide dimer is a complex formed by two peptide chains (peptides or proteins) joined together by chemical bonds (usually covalent or non-covalent). It consists of two identical or different peptide units, which can be of the same amino acid sequence or different amino acid sequences.
Fig. 1. Synthesis of chemically linked peptide dimers (Proceedings of the National Academy of Sciences. 2003, 100(8): 4435-4439).
Functions of Peptide Dimers
- Enhancement of Activity
Peptide dimers may exhibit enhanced biological activity or function over a single peptide chain, such as having higher anti-microbial activity, stronger cell signaling ability, or higher receptor binding affinity. - Altered Specificity and Selectivity
Peptide dimers can increase the ability to recognize and bind to a specific receptor, target or ligand and improve its selectivity. - Expanded Target Range
This dual or multiple binding ability expands the target range of peptide dimers, allowing them to modulate the function of multiple targets simultaneously, resulting in a broader range of biological activities. - Signal Regulation
Peptide dimers can be used to modulate intracellular signaling pathways. By connecting peptide units with different functions, the activation or inhibition of signaling pathways can be altered, thus regulating the physiological processes and functions of cells. - Structural Stability
Linking two peptide units enhances the structural stability of the peptide molecule. Peptide dimers are generally more stable than individual peptide chains and are more resistant to changes in environmental conditions, thus prolonging their biological activity and functional persistence.
Formation of Peptide Dimer
Covalent Linkage
- Peptide bonding: Two peptide chains are linked together by a covalent peptide bond to form a peptide dimer. This type of linkage usually requires the introduction of an appropriate functional group, such as an amino or hydroxyl group, at both ends of the peptide chain in order to form the peptide bond.
- Crosslinker linkage: A cross-linker is a compound that reacts with a specific functional group in the peptide chain to form a covalent bond, e.g., a disulfide cross-linker reacts with a cysteine residue to form a disulfide bond, thus joining the two peptide chains.
Non-covalent Linkages
- Hydrogen bonding: Hydrogen bonding in peptide chains can encourage two peptide chains to come closer to each other and form a peptide dimer. Hydrogen bonds are formed through interactions between hydrogen atoms and atoms with high electronegativity such as nitrogen, oxygen or fluorine.
- Hydrophobic interactions: Hydrophobic interactions are due to the fact that the hydrophobic side chains of hydrophobic amino acids tend to aggregate in an aqueous environment, thus binding the two peptide chains together.
- Ionic bonding: Charged amino acid residues in a peptide chain (e.g., lysine, glutamic acid, etc.) can be attracted to residues of opposite charge, forming ionic bonding connections.
- Van der Waals forces: Van der Waals force interactions between two peptide chains can promote the formation of peptide dimers. Van der Waals force is the mutual attraction between transient dipoles due to the uneven distribution of electron clouds between molecules.
Applications of Peptide Dimers
- Receptor Agonist/Antagonist
Peptide dimers can mimic the action of natural ligands or drugs as agonists or antagonists of receptors. By linking two peptide units, the receptor binding affinity can be enhanced, improving drug selectivity and potency. - Biosensors
By linking two peptide chains with the ability to recognize a specific molecule, signal amplification and detection sensitivity can be enhanced for the detection of drugs, metabolites, biomarkers, and more. - Cell Signaling Regulation
Peptide dimers connect two functionally different peptide chains together and can regulate the activation or inhibition of intracellular signaling pathways, thereby affecting the physiological processes of cells. - Protein Structure Studies
Peptide dimers can change the conformation and stability of proteins, thereby revealing the structure-function relationship and interaction mechanism of proteins. - Antibody Engineering
Peptide dimers connecting two antibody units can form bispecific antibodies, which can bind different antigens at the same time and improve the therapeutic effect of antibodies.
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Reference
- Schäffer, L. et al. Assembly of high-affinity insulin receptor agonists and antagonists from peptide building blocks. Proceedings of the National Academy of Sciences. 2003, 100(8): 4435-4439.
