Abstract
We report the orientational behavior of nematic liquid crystals (LCs) influenced by a cyclic lipopeptide, polymyxin B (PmB). It was found that PmB can spontaneously self-assemble at aqueous-LC interfaces and induce a homeotropic ordering of the LCs at those interfaces, thus resulting in dark optical appearance of the LC under cross polarizers. Density functional theory studies substantiate the experimental findings that the stability of homeotropic anchoring of the LC is strongly influenced by the hydrophobic interactions between aliphatic tails of PmB and LC molecules along with the additional supramolecular interactions between their head groups. Interestingly, exposure of the PmB-laden aqueous-LC interface to anionic serum proteins such as bovine serum albumin (BSA) and human hemoglobin triggered a planar reorientation of the LC, leading to a bright optical state of the LC. This allows label-free characterization of the biomolecular interactions between proteins and antibiotics (i.e., PmB) in vitro at ...
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