title: Fabrication of ovalbumin-phospolipid thin film with minimal protein aggregation by different self-assembly methods.
abstract: This paper describes a new approach for the preparation of Ovalbumin (OVA)-phospholipids (DPPC) thin film, where we minimize the aggregation among protein molecules. A comparative study on the films fabricated by self-assembly (SA) of protein-lipid mixed vesicle on hydrophilic glass substrate and SA of protein alone on prefabricated Langmuir-Blodgett (LB) film of DPPC is being carried out. Far UV circular dichroism spectroscopy, FTIR analysis of amide bands and surface morphology study by FE-SEM imaging is being used to examine the extent of conformational change as well as aggregation of protein. Protein-lipid thin film prepared by the former method provides the secondary structure of individual OVA molecules with increment of alpha-helical segments. In this process, OVA molecules do not show larger aggregation among themselves. However, in the second method, we find unfolded larger aggregated structure of OVA with increment of beta-structure of OVA.
authors.affiliation: Department of Spectroscopy, Indian Association for the Cultivation of Science, Jadavpur, Kolkata 700032, India.
authors.forename: Tapanendu
authors.initials: T
authors.lastname: Kamilya
authors.forename: Prabir
authors.initials: P
authors.lastname: Pal
authors.forename: Mrityunjoy
authors.initials: M
authors.lastname: Mahato
authors.forename: G B
authors.initials: GB
authors.lastname: Talapatra
mesh_terms: D015060:1,2-Dipalmitoylphosphatidylcholine / Q000737:chemistry*; D002942:Circular Dichroism; D008081:Liposomes / Q000737:chemistry; D010047:Ovalbumin / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
chemical_list: D008081:Liposomes; D015060:1,2-Dipalmitoylphosphatidylcholine; D010047:Ovalbumin