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Covalent Bonds

Covalent Bonds

Covalent Bonds

Covalent Bonds

Overview
When two atoms share electrons to complete their valence shells, they create a covalent bond. An atom's electronegativity—the force with which shared electrons are pulled towards an atom—determines how the electrons are shared. Molecules formed with covalent bonds can be either polar or nonpolar. Atoms with similar electronegativities form nonpolar covalent bonds; the electrons are shared equally. Atoms with different electronegativities share electrons unequally,...

Network Covalent Solids

Network Covalent Solids

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.
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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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....

Covalent Bonding and Lewis Structures

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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.

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Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.

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Related Experiment Video

Updated: Feb 4, 2026

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay

Published on: February 28, 2025

An Internally Controlled Quantitative Target Occupancy Assay for Covalent Inhibitors.

Rasmus Hansen¹, Sarah J Firdaus², Shuangwei Li²

¹Wellspring Biosciences, Inc., 3033 Science Park Rd., Ste. 220, San Diego, CA, 92121, USA. rasmus@wellspringbiosciences.com.

Scientific Reports

|September 27, 2018

Summary

This summary is machine-generated.

A new mass spectrometry method quantifies target occupancy for covalent inhibitors without needing untreated controls. This approach was successfully applied to assess the KRAS^G12C inhibitor ARS-1620.

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Last Updated: Feb 4, 2026

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Area of Science:

Pharmacology
Biochemistry
Analytical Chemistry

Background:

Target occupancy assessment is vital for evaluating novel inhibitors' efficacy.
Current clinical methods for target occupancy require untreated controls, posing challenges.
Covalent inhibitors require robust target engagement confirmation.

Purpose of the Study:

To develop a novel mass spectrometry method for quantitative target occupancy assessment.
To enable target occupancy measurement without the need for untreated controls.
To apply the developed method to a specific KRAS^G12C inhibitor, ARS-1620.

Main Methods:

Quantitative mass spectrometry approach.
Development of a method for target occupancy analysis.
Application to KRAS^G12C inhibitor ARS-1620.

Main Results:

A novel mass spectrometry method was successfully established.
The method allows quantitative target occupancy assessment without untreated controls.
The method was validated using the KRAS^G12C inhibitor ARS-1620.

Conclusions:

The developed mass spectrometry technique offers a viable alternative for target occupancy assessment.
This method simplifies the evaluation of covalent inhibitors in clinical settings.
It facilitates proof-of-mechanism studies and dose determination for novel inhibitors.