Tuning Electrostatic Interactions To Control Orientation of GFP Protein Adsorption on Silica Surface.
ACS Appl Bio Mater
; 7(2): 596-608, 2024 Feb 19.
Article
in En
| MEDLINE
| ID: mdl-37347172
ABSTRACT
The adsorption of green fluorescent protein (GFP) on silica surfaces has been the subject of growing interest due to its potential applications in various fields, including biotechnology and biomedicine. In this study, we used all-atom molecular dynamics simulations to investigate the charge-driven adsorption of wild type GFP and its supercharged variants on silica surfaces. The results showed that the positively charged variant of GFP adsorbed on the negatively charged silica surface with minimal loss in its secondary structure. Further studies were conducted to understand the role of surface charge distribution on two other positively charged variants of GFP, and the results showed that the orientation of GFP on silica can be easily tuned by careful mutations of the charged amino acid residues on the GFP. This study provides valuable molecular insights into the role of electrostatic-driven adsorption of GFP and highlights the importance of charge interactions in the adsorption process.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Silicon Dioxide
Language:
En
Journal:
ACS Appl Bio Mater
Year:
2024
Document type:
Article
Affiliation country:
India