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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Published in | Current opinion in colloid & interface science Vol. 42; pp. 157 - 168 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Elsevier Ltd
01.08.2019
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Subjects | |
Online Access | Get full text |
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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.
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ISSN: | 1359-0294 1879-0399 |
DOI: | 10.1016/j.cocis.2019.08.001 |