Protein adsorption at solid-liquid interfaces plays an important role in many biomedical applications. Biomaterials, protein microarrays, and lab-on-a-chip devices all rely on this phenomenon. Due to the importance of protein adsorption in academia and industry alike, there has been a large effort in attempting to quantify this process. Various experiments have been performed to gain a better understanding of protein-surface interactions, with the hopes of eventually being able to accurately predict and model surface adsorption behaviour.
The Biomolecular Adsorption Database (BAD) is collection of protein adsorption data aggregated from various published sources. The main aim of this project is to provide easy access to the abundance of surface adsorption data available in literature. By localizing this comprehensive dataset into a common hub, we hope to reduce the tediousness of data collection. To read more about the BAD project, click here.
The BAD dataset can be viewed below. The table can be filtered, sorted, and searched. On the backend, the information has been stored in a MySQL database. As its purpose is to serve as an open-source database, BAD is continuously evolving as new data is published. We also welcome new entries. If interested in contributing, please contact the lab for more information regarding submission guidelines.
Proteins: BAD comprises a variety of representative proteins. For each protein, the PDB (Protein DataBase) is provided, as well as basic structural descriptors, including its molecular weight, isoelectric point, total residues (and number of alpha and beta residues), and the number of disulfide bonds it possesses. Furthermore, based on these primary values, “rigidity” is computed as [(alpha + beta + 2*SS bonds) / total residues].
Surface variables: BAD primarily describes surface hydrophobicity via surface tension (mJ/m^2)^2 and contact angle (degrees).
Solution variables: BAD reports the conditions of the buffer solutions used for each adsorption experiment. In particular, temperature (Celsius), pH, and ionic strength are recorded in the database. A column which measures the absolute difference in pH and isoelectric point (IP) can also be found in the table.
Protein concentration: BAD provides the protein concentration on both the adsorbing surface (mg/m^2) and in the buffer solution (mg/ml). Lastly, for each entry, the measurement method used for the experiment is listed. For a description of the different experiment types, please refer to the original BAD paper.
Connection to ProMS: the proteins included in BAD have been analyzed using ProMS. The resulting surface properties for each unique protein can be found on the ProMS page. Protein properties calculated on the molecular surfaces are presented in descriptors of the BAD proteins.
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