Abstract
In this Article, we report the surface activity of the human globular blood protein, hemoglobin (Hb), at the air/water interface. The Langmuir-Blodgett technique is used for monolayer characterization. The adsorption growth-kinetics study shows that the adsorption process at the air/water interface is involved with two mechanisms: one diffusion with adsorption and the other rearrangement with unfolding. The kinetics is found to be dependent on pH and protein concentration in the subphase. The CD and FTIR studies suggest larger intermolecular aggregate and beta-sheet formation in the film lifted from the air/acidic water subphase. In alkaline pH and in isoelectric pH (6.8), not much variation is observed. The FE-SEM images support this observation. The acidic pH induced such conformational changes, and aggregation is explained with the argument of alpha-helix to beta-sheet conversion as well as the competition between protonation and deprotonation of the aromatic-amino acid residues at the air/water interface.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
