This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Proteins with exposed arginine can selectively accumulate even on protein-resistant coatings, as reported by researchers from Science Tokyo. Through an in-depth analysis of which proteins adhere and how they adhere to various anti-fouling surfaces, the team found that arginine disrupts the protective water layer that normally blocks adsorption.
Their results will help scientists develop safer and more effective biocompatible materials for medical devices, such as stents and advanced biosensors. When a medical device enters the body, whether it's an implant, a catheter or a biosensor, it immediately gets coated with proteins from bodily fluids. This protein layer, known as the protein corona, is what the body mainly interacts with rather than the material underneath.
Therefore, the corona is what the immune system and surrounding tissues "see" first; it plays a major role in determining whether a material is biocompatible or whether it will trigger unwanted reactions such as inflammation. To reduce these risks, scientists have developed several "anti-fouling" coatings. By holding a tightly bound layer of water at the material's surface, these coatings can block proteins from sticking.
However, in real biological fluids such as blood serum, some proteins still manage to accumulate even on these supposedly resistant surfaces. Predicting which proteins can bypass anti-fouling protection has remained a major challenge. To address this knowledge gap, a research team including Associate Professor Tomohiro Hayashi, master's course student Ayano Nomura and colleagues from the Department of Material Science and Engineering, School of Materials and Chemical Technology, Institute of Science Tokyo (Science Tokyo), Japan, collaborated with Kyocera Corporation, Japan, to identify what happens at the molecular level on anti-fouling surfaces.
Their study, published online in the journal Advanced Materials Interfaces on Aug. 24, 2026, combined high-sensitivity proteomics with protein structural analysis to examine the protein corona formed from human serum on six model organic surfaces, including widely used anti-fouling coatings. The researchers first measured how much serum protein adsorbed onto each surface and then identified the specific proteins present using nano liquid chromatography–tandem mass spectrometry. More than 200 proteins were identified on each surface, allowing the researchers to compare not just the total amount of protein adsorption but also the detailed composition of the corona.
The team then checked whether factors such as molecular weight or isoelectric point could explain which proteins accumulated on these protein-resistant surfaces. However, they found that these conventional indicators were not enough. Instead, statistical analysis revealed one feature that clearly distinguished proteins that accumulated from those that were excluded: the proportion of arginine residues exposed on the protein surface.
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