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Updated: Oct 14, 2025

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
Published on: April 23, 2017
Distinct interfacial ordering of liquid crystals observed by protein-lipid interactions that enabled the label-free
Manisha Devi1, Indu Verma1, Santanu Kumar Pal1
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali (IISERM), Knowledge City, Sector-81, SAS Nagar, Mohali 140306, India. skpal@iisermohali.ac.in.
Abstract:
Interfaces formed between a lipid decorated liquid crystal (LC) film and an aqueous phase can mimic the bimolecular membrane where interfacially occurring biological phenomena (e.g., lipid-protein interactions, protein adsorption) can be visually monitored by observing the surface-sensitive orientations of LCs. The ordering behavior of LCs at different phospholipid-based LC interfaces (1,2-dilauroyl-sn-glycero-3-phosphocholine (DLPC) and lysophosphatidic acid (LPA)) were investigated to determine the sensing of an important cytoplasmic protein (juxtamembrane of epidermal growth factor receptor (JM-EGFR)). At both DLPC and LPA decorated interfaces, the LC adopts homeotropic ordering, causing a dark optical appearance under crossed polarizers. Interestingly, upon the introduction of JM-EGFR to these LC-aqueous interfaces, the homeotropic orientation of the LC changed to planar (bright optical appearance), suggesting the potential of the designed system for JM-EGFR sensing. The use of different lipid decorated LC-aqueous interfaces results in the emergence of distinct optical patterns. For example, at a DLPC laden interface, elongated bright domains are observed, whereas a uniform bright texture is observed on an LPA laden interface. The DLPC decorated LC-aqueous interface is found to be highly selective for the sensing of JM-EGFR with a detection limit in the nanomolar concentration region (∼ 50 nM). When compared to spectroscopic and other conventional techniques, the LC-based design is simpler, and it allows the simple and label-free optical sensing of JM-EGFR at fluidic interfaces.

