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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

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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.
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Related Experiment Video

Updated: Feb 7, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Reversible covalent direct thrombin inhibitors.

Mohanram Sivaraja¹, Nicola Pozzi², Matthew Rienzo¹

¹Verseon Corporation, Fremont, California, United States of America.

|August 3, 2018

Summary

This summary is machine-generated.

A new class of direct thrombin inhibitors (VE-DTIs) offers a novel approach to anticoagulation. Compound 1, a VE-DTI, demonstrates potent and selective thrombin inhibition with a unique reversible covalent mechanism, potentially improving efficacy and bleeding profiles.

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Last Updated: Feb 7, 2026

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Area of Science:

Pharmacology
Biochemistry
Medicinal Chemistry

Background:

Traditional anticoagulants like heparin and warfarin are being superseded by novel oral anticoagulants.
Novel oral anticoagulants offer convenience but have contraindications and significant bleeding risks.

Purpose of the Study:

To characterize the mechanism of action and in vitro pharmacology of Compound 1, a novel direct thrombin inhibitor (VE-DTI).

Main Methods:

Kinetics, biochemical assays, and X-ray structural studies were employed.
In vitro pharmacology was assessed using various assays, including thrombin inhibition, substrate activity, and clotting assays.

Main Results:

Compound 1 acts via reversible covalent inhibition, potently and selectively inhibiting thrombin.
It demonstrated nanomolar potency against free and clot-bound thrombin and inhibited thrombin generation with low micromolar potency.
The compound showed a distinct pharmacological profile in clotting assays, with weak inhibition in PT and aPTT.

Conclusions:

Compound 1, a VE-DTI, exhibits a unique reversible covalent inhibition mechanism.
This novel mechanism offers a differentiating pharmacological profile with potential for improved anticoagulant efficacy and bleeding profiles.