Structural characterization of protein–polymer conjugates for biomedical applications with small-angle scattering

Protein–polymer conjugates, typically consisting of one or more polymers covalently attached to a protein, are an increasingly common component in biotechnology. Polymers can increase circulation time, alter immune responses, and influence the self-assembly of proteins to which they are attached. To...

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Bibliographic Details
Published inCurrent opinion in colloid & interface science Vol. 42; pp. 157 - 168
Main Authors Pokorski, Jonathan K., Hore, Michael J.A.
Format Journal Article
LanguageEnglish
Published Elsevier Ltd 01.08.2019
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Summary:Protein–polymer conjugates, typically consisting of one or more polymers covalently attached to a protein, are an increasingly common component in biotechnology. Polymers can increase circulation time, alter immune responses, and influence the self-assembly of proteins to which they are attached. To understand and take full advantage of the benefits that protein–polymer conjugates provide, there is a strong need for structural characterization of both the conjugates and their self-assembled structures. Although X-ray crystallography is suitable for determining protein structure, protein–polymer conjugates do not generally crystallize, requiring the use of alternative techniques. Small-angle scattering, with neutrons in particular, is one such technique. In this article, we review recent work in the area of protein–polymer conjugates and highlight the important role that structure plays. We then highlight shape-dependent and shape-independent approaches for structural characterization of protein–polymer conjugates and future directions in small-angle scattering interpretation. We conclude by introducing a new model that we suggest may be useful in the future to acquire more detailed structural properties. [Display omitted]
ISSN:1359-0294
1879-0399
DOI:10.1016/j.cocis.2019.08.001