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A Comparative Study of the Phase Separation of a Nematic Liquid Crystal in the Self-assembling Drying Protein Drops

Published online by Cambridge University Press:  10 April 2019

Anusuya Pal ,
Amalesh Gope  and
Germano S. Iannacchione
Anusuya Pal
Affiliation:
Order-Disorder Phenomena Laboratory, Department of Physics, Worcester Polytechnic Institute, Worcester, MA, 01609, USA
Amalesh Gope
Affiliation:
Department of English and Foreign Languages, Tezpur University, Tezpur, Assam, 784028, India
Germano S. Iannacchione*
Affiliation:
Order-Disorder Phenomena Laboratory, Department of Physics, Worcester Polytechnic Institute, Worcester, MA, 01609, USA
*
*(Email: gsiannac@wpi.edu)
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Abstract

The drying process, self-assembly of the proteins and the phase separation of a thermotropic liquid crystal (LC) from an initial aqueous solution represent a rich area of study. A focus of this work is to compare the behavior of two different proteins, bovine serum albumin [BSA] and lysozyme [Lys] in the ternary system through optical microscopy. During the drying process, the intensity profile shows three regimes in the presence of LC whereas no intensity variation is observed in its absence in both protein drops. The striking outcome is the presence of an umbilical defect of [+1] strength in every domain near the edge of BSA drop, whereas, each domain has a central dark region surrounded by a bright region in the dried Lys drop. Finally, the crack spacing in the dried Lys drop is reduced in the presence of LC whereas, no significant difference is found in the dried BSA drop.

Keywords

self-assemblyliquid crystalmorphology
Type
Articles
Information
MRS Advances , Volume 4 , Issue 22: Biomaterials and Soft Materials , 2019 , pp. 1309 - 1314
Copyright
Copyright © Materials Research Society 2019 

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References

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