Abstract
One of the most important classes of proteins in terms of drug targets is cell surface membrane proteins, and yet it is a challenging set of proteins for generating high-quality affinity reagents. In this review, we focus on the use of phage libraries, which display antibody fragments, for generating recombinant antibodies to membrane proteins. Such affinity reagents generally have high specificity and affinity for their targets. They have been used for cell staining, for promoting protein crystallization to solve three-dimensional structures, for diagnostics, and for treating diseases as therapeutics. We cover publications on this topic from the past 10 years, with a focus on the various formats of membrane proteins for affinity selection and the diverse affinity selection strategies used. Lastly, we discuss the challenges faced in this field and provide possible directions for future efforts.
Highlights
Recombinant affinity reagents offer many practical advantages compared to polyclonal or monoclonal antibodies [1]
Theseand challenges have led to a number of the innovative for difficult to overexpress in large amounts, their stability normally requires presencemethods of artificial formatting membrane proteins targets forhave phage-display experiments and affinity selection
G-protein coupled coupled receptors receptors (GPCRs) mutants with higher expression and stability engineered by the above three methods are useful for crystallization [51,52], biophysical characterization, and drug screening [53]
Summary
Recombinant affinity reagents offer many practical advantages compared to polyclonal or monoclonal antibodies [1]. One to class of targets that has been very librariestohave improved It is straightforward generate a recombinant affinity challenging for phage-display experiments is the membrane protein. These proteins are reagent to virtually any soluble and well-folded proteins. One class of targets that has been very difficult to overexpress in large amounts, is and stability normally requiresthese the proteins presenceare of challenging for phage-display experiments thetheir membrane protein. Theseand challenges have led to a number of the innovative for difficult to overexpress in large amounts, their stability normally requires presencemethods of artificial formatting membrane proteins targets forhave phage-display experiments and affinity selection
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