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Covalently Linked Protein Regulators

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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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Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Updated: May 22, 2026

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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Published on: September 28, 2022

Controlling morphology of peptide-based soft structures by covalent modifications.

Nidhi Gour¹, Apurba K Barman, Sandeep Verma

¹Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur-208 016 UP, India.

Journal of Peptide Science : an Official Publication of the European Peptide Society

|April 27, 2012

Summary

Modifying diphenylalanine (FF) with mannose or thiol groups controls its self-assembly. Mannose attachment alters morphology from tubes to spheres, while thiol introduction also induces spherical structures, enabling lectin interactions.

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Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Area of Science:

Soft matter physics
Supramolecular chemistry
Biomaterials science

Background:

Controlling the morphology of self-assembling soft matter is crucial for developing advanced materials.
Diphenylalanine (FF), a motif from amyloid-beta, self-assembles into tubular structures.
Covalent modification offers a route to tune self-assembly behavior.

Purpose of the Study:

To investigate the effect of mannose and thiol functionalization on the self-assembly of diphenylalanine (FF).
To explore the potential of these modified peptides in lectin-binding applications.

Main Methods:

Covalent conjugation of mannose residues and thiol functionalities to the FF dipeptide.
Analysis of the solution-phase self-assembly process and resulting morphologies.
Assessment of glycopeptide interaction with concanavalin A.

Main Results:

Attachment of a single mannose residue to FF retained tubular structures.
Conjugation of two mannose units or introduction of a thiol group induced a switch to spherical morphology.
Glycopeptides demonstrated interaction with concanavalin A, indicating accessible mannose units.

Conclusions:

Covalent modification of FF with mannose or thiol groups effectively controls its self-assembly morphology.
The resulting glycopeptides are capable of lectin-carbohydrate interactions in their self-organized state.
This study provides insights into designing functional soft matter through peptide modification.