Molecular insight into affinity interaction between cibacron blue and proteins
Publikationstyp
Journal Article
Date Issued
2017-08-03
Sprache
English
Institut
TORE-URI
Volume
56
Issue
34
Start Page
9691
End Page
9697
Citation
Industrial and Engineering Chemistry Research 34 (56): 9691-9697 (2017-08-30)
Publisher DOI
Scopus ID
Publisher
American Chemical Society (ACS)
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.
DDC Class
570: Biowissenschaften, Biologie
620: Ingenieurwissenschaften
More Funding Information
Supported by the German Research Foundation (Project No. FI 1452/7-1).