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Protein−nanoparticle (NP) complexes are nanomaterials that have numerous potential uses ranging from biosensing to biomedical applications such as drug delivery and nanomedicine. Despite their extensive use quantifying the number of bound proteins per NP remains a challenging characterization step that is crucial for further developments of the conjugate, particularly for metal NPs that often interfere with standard protein quantification techniques. In this work, we present a method for quantifying the number of proteins bound to pegylated thiol-capped gold nanoparticles (AuNPs) using an infrared (IR) spectrometer, a readily available instrument. This method takes advantage of the strong IR bands present in proteins and the capping ligands to quantify protein−NP ratios and circumvents the need to degrade the NPs prior to analysis. We show that this method is generalizable where calibration curves made using inexpensive and commercially available proteins such as bovine serum albumin (BSA) can be used to quantify protein−NP ratios for proteins of different sizes and structures.more » « lessFree, publicly-accessible full text available February 26, 2025
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Characterizing protein–surface and protein–nanoparticle conjugates: Activity, binding, and structureMany sensors and catalysts composed of proteins immobilized on inorganic materials have been reported over the past few decades. Despite some examples of functional protein–surface and protein–nanoparticle conjugates, thorough characterization of the biological–abiological interface at the heart of these materials and devices is often overlooked in lieu of demonstrating acceptable system performance. This has resulted in a focus on generating functioning protein-based devices without a concerted effort to develop reliable tools necessary to measure the fundamental properties of the bio–abio interface, such as surface concentration, biomolecular structure, and activity. In this Perspective, we discuss current methods used to characterize these critical properties of devices that operate by integrating a protein into both flat surfaces and nanoparticle materials. We highlight the advantages and drawbacks of each method as they relate to understanding the function of the protein–surface interface and explore the manner in which an informed understanding of this complex interaction leads directly to the advancement of protein-based materials and technology.more » « less