Covalent Binding
Covalent Binding - Related Videos
02:18
Network Covalent Solids
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2020
Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds. To break or to melt a covalent network solid, covalent bonds must be broken. Because covalent bonds are relatively strong, covalent network solids are typically...
02:04
Covalently Linked Protein Regulators
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2020
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified. These groups modify specific amino acids in a protein.
10:23
Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach
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Cited by 8 •
2013
We describe a method for accomplishing efficient immobilization of BMP-2 on surfaces. Our approach is based on the formation of a self-assembled monolayer to achieve the covalent binding of BMP-2 via its free amine residues. This method is a useful tool to study signaling at the cell membrane.
02:46
Covalent Bonding and Lewis Structures
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2020
Compared to ionic bonds, which results from the transfer of electrons between metallic and nonmetallic atoms, covalent bonds result from the mutual attraction of atoms for a “shared” pair of electrons. Covalent bonds are formed between two atoms when both have similar tendencies to attract electrons to themselves (i.e., when both atoms have identical or fairly similar ionization energies and electron affinities). Physical Properties of Covalent Compounds Compounds that contain covalent...
02:18
The Equilibrium Binding Constant and Binding Strength
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2020
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium: where P and L are the unbound protein and ligand, respectively, and PL is the protein-ligand complex. As the amount of bound ligand is also related to the rate of ligand binding, experiments can also determine Kb by examining the rates of protein-ligand association (kon) and dissociation (koff) using the following ratio: Thus,...
FAQs
The key chemical step occurs when an electrophilic group on a drug reacts with a nucleophilic site on a biological target. In pharmacology, relevant nucleophiles can include cysteine, lysine, or serine residues on proteins. Which residue is modified depends on the available reactive groups, influencing the resulting drug-target adduct and the selectivity of the pharmacological effect.
A covalent drug-target adduct may remain after concentrations of unbound drug decline. Because the target can stay chemically modified, pharmacological suppression may persist beyond the period when free drug is readily available. This durability can extend the functional effect, although it also makes the consequences of unintended target modification more important for safety assessment.
Selective covalent binding favors a particular biological target and supports a defined pharmacological response, whereas nonspecific reactions can modify unrelated proteins. The distinction depends on balancing the drug’s electrophilic reactivity with appropriate target recognition. Strong reactivity without sufficient selectivity may create multiple protein adducts, increasing the possibility of altered protein function and adverse drug responses.
Evaluation requires balancing therapeutic duration and target suppression against chemical reactivity and safety. A reaction that preserves target inhibition may be useful when it produces a stable, intended adduct, but excessive or poorly directed reactivity can affect other proteins. This balance guides assessment of whether covalent binding contributes a controlled pharmacological benefit or an unacceptable toxicity risk.
Targeted covalent inhibitors are designed to maintain durable suppression of a selected biological target. Their strategy combines target-directed recognition with an electrophilic drug group capable of reacting with a nucleophilic residue. The resulting persistent adduct can support prolonged pharmacological activity, making covalent binding relevant to drug designs that seek effects lasting beyond declining free-drug concentrations.
Covalent binding studies help determine whether a drug modifies only its intended target or also reacts with unrelated proteins. Nonspecific protein alteration may contribute to toxicity or adverse drug responses, so researchers examine chemical reactivity alongside pharmacological duration and selectivity. This context is especially important when a stable adduct could persist after systemic free drug levels fall.