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  Balancing soft elasticity and low surface polarity in films of charged BSA capsules at air/fluid interface

Madhumitha, D., Jaganathan, M., Dhathathreyan, A., & Miller, R. (2016). Balancing soft elasticity and low surface polarity in films of charged BSA capsules at air/fluid interface. Colloids and Surfaces B: Biointerfaces, 146, 161-170. doi:10.1016/j.colsurfb.2016.06.007.

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 Creators:
Madhumitha, D., Author
Jaganathan, Maheshkumar, Author
Dhathathreyan, Aruna, Author
Miller, Reinhard1, Author           
Affiliations:
1Reinhard Miller, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863501              

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Free keywords: Protein capsules
 Abstract: Interaction between charged BSA colloids and the buffer at air/fluid interface has been studied using spread films of the capsules of the protein prepared at pH 4.5 and 7.5 (below and above the pI of BSA). Surface pressure-surface concentration plots, interfacial dilational rheology and Quartz crystal microbalance with dissipation have been used to characterize the films. The study shows that below the pI of the protein, the positively charged colloids entrain more water on the surface which leads to partial neutralization of the charges. Results suggest that the charged capsules are elastic due to the strongly adsorbed protein layers that restrict deformation and any small shape fluctuations is likely due to the distortion of the viscoelastic surface layer at pH = 4.5. Capsules of BSA behave as ‘soft elastic membrane’ with interfacial properties lying between that of an elastic membrane and a slightly soluble diffuse capsule with low interfacial tension. Such elastic capsules would find applications in drug delivery and food colloids.

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 Dates: 2016-06-032016
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1016/j.colsurfb.2016.06.007
BibTex Citekey: D2016
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Title: Colloids and Surfaces B: Biointerfaces
  Abbreviation : Colloids Surf., B
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 146 Sequence Number: - Start / End Page: 161 - 170 Identifier: ISSN: 0927-7765