Nature endowed structurally and functionally complex transmembrane proteins to adequately maintain the ion trafficking across the membrane to ensure healthy physiological functions. mutations occurring in these intrinsic transmembrane proteins are implicated in a variety of pathologies that are collectively referred to as channelopathies.Â
Consequently, elucidating the structural intricacies and ion translocation mechanisms of these inherent transmembrane proteins motivates the scientific community to engineer synthetic scaffolds capable of replicating the functionalities of these natural transmembrane proteins, not only to gain insights into their structural and functional characteristics but also to explore diverse biomedical applications.
Numerous synthetic molecules have been developed to transport cations or anions and imitate both the structure and function of natural ion transport systems to address the structural and functional complexity of natural ion channels. However, synthetic cation-anion symporter channels have received limited attention due to difficulties in decorating the channel selectivity filter to transport both cation and anion selectively. Hence, despite efforts to create a channel with single ion selectivity in a lipid bilayer by artificial channels, a general synthetic strategy for realizing more complex dual ion selectivity is challenging to propose.
My research is focused on the designing of gated and non-gated ion carriers and ion channels for transmembrane cation-anion and proton transport by utilizing different core motifs. Additionally, in the thrust of the knowledge, I actively explored the decoration of the synthetic ion channel systems for transmembrane transport of the water and also decorating different small molecule-based synthetic transporter systems that can be localized in the particular organelles to kill the cancer cells accurately.