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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Reactivity and Selectivity Principles in Native Protein Bioconjugation.

Ramesh Adakkattil1, Kalyani Thakur1, Vishal Rai1

  • 1Department of Chemistry, Indian Institute of Science Education and Research Bhopal, Bhopal Bypass Road, Bhauri, 462 066, Bhopal, Madhya Pradesh, India.

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|June 29, 2021
PubMed
Summary

This research explores chemical methods for precise protein engineering, developing platforms for controlled chemoselectivity and site-specificity. Key innovations include modular linchpin directed modification (LDM®) and Gly-tag® technology for advanced bioconjugate analysis.

Keywords:
Antibody-drug conjugatesBioconjugationChemoselectivityProtein-specificitySite-selectivitySite-specificity

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Area of Science:

  • Chemical Biology
  • Protein Engineering
  • Bioconjugation

Background:

  • Precise engineering of native proteins using chemical methods remains a challenge.
  • Developing platforms for controlled chemoselectivity, site-selectivity, and modularity is crucial for protein modification.
  • Site-specificity and protein-specificity are key requirements for advanced bioconjugation applications.

Purpose of the Study:

  • To review a decade of research on chemical methods for precise protein engineering.
  • To present novel platforms for regulating chemoselectivity, site-selectivity, and modularity in protein modification.
  • To highlight tools for analyzing bioconjugates, particularly for homogeneous antibody-drug conjugates (ADCs).

Main Methods:

  • Development of chemoselective and site-selective labeling strategies targeting protein reactivity hotspots.
  • Introduction of modular linchpin directed modification (LDM®) platform.
  • Implementation of site-specific Gly-tag® technology.

Main Results:

  • Demonstrated precise chemoselective and site-selective labeling of proteins.
  • Established LDM® as a versatile platform for protein modification.
  • Developed and applied Gly-tag® technology for site-specific bioconjugation.
  • Utilized Maspecter® and other tools for detailed bioconjugate analysis, including homogeneous ADCs.

Conclusions:

  • Chemical methods can achieve precise engineering of native proteins.
  • Novel platforms like LDM® and Gly-tag® empower regulation of selectivity and specificity.
  • Advanced analytical tools facilitate the development of sophisticated bioconjugates such as homogeneous ADCs.