Industrial & Engineering Chemistry Research
Industrial & Engineering Chemistry Research
5 years ago

Molecular Insight into Affinity Interaction between Cibacron Blue and Proteins

Molecular Insight into Affinity Interaction between Cibacron Blue and Proteins
Georg Fieg, Thomas Waluga, Juan Liang-Schenkelberg
Molecular dynamics (MD) simulations with all-atom models combining adsorption experiments are used to gain a better understanding of affinity interaction between proteins and Cibacron Blue (CB). These interactions with three different proteins are studied. The interactions with CB of different proteins are varying, although HSA and BSA have very similar structures. The influence of pH and salt concentration on these protein–CB bindings is investigated. Different parts of the CB molecule play miscellaneous roles in these interactions. The triazine part plays an important role in the hydrogen bonding between CB and bHb. The binding sites on protein surface differ by changing pH, salt concentration, and protein types. However, two parts seem to be very important to the binding of serum albumins.

Publisher URL: http://dx.doi.org/10.1021/acs.iecr.7b01556

DOI: 10.1021/acs.iecr.7b01556

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.