Quinn, Michelle K. and James, Susan and McManus, Jennifer J. (2019) Chemical Modification Alters Protein–Protein Interactions and Can Lead to Lower Protein Solubility. The Journal of Physical Chemistry B, 123 (20). pp. 4373-4379. ISSN 1520-6106

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Abstract

The chemical modification of proteins is at the frontier of developments in biological imaging and biopharmaceutics. With the advent of more sensitive and higher resolution imaging techniques, researchers increasingly rely on the functionalization of proteins to enable these techniques to capture cellular processes. For biopharmaceutical therapies, chemically modified proteins, for example, antibody-drug conjugates (ADCs) offer the possibility of more tailored treatments for the disease with lower toxicities than traditional small molecule therapies. However, relatively little consideration is paid to how chemical modifications impact protein–protein interactions and solution stability. Using human γD-crystallin as a model, we demonstrate that chemical modification of the protein surface alters protein–protein interactions, which can result in lower solubility depending on the chemical nature of the modifier and the position on the protein where the modification is made. Understanding these effects is essential to ensure that modifying proteins effectively occurs with minimum self-association and that studies carried out using labelled proteins accurately reflect those of unmodified proteins.

Item Type:	Article
Keywords:	Chemical modification; Mixtures; Modification; Monomers; Peptides; proteins;
Academic Unit:	Faculty of Science and Engineering > Chemistry
Item ID:	16194
Identification Number:	https://doi.org/10.1021/acs.jpcb.9b02368
Depositing User:	Jennifer Mc Manus
Date Deposited:	29 Jun 2022 07:44
Journal or Publication Title:	The Journal of Physical Chemistry B
Refereed:	Yes
URI:	Publisher
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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