Molecular Design Of Lanthanide Binding Tag Peptides For Nanoparticle Assisted Interfacial Separation Of Rare Earth Elements
type: CreativeWork
description: Rare earth elements (REEs), comprising yttrium, scandium, and the lanthanides, are indispensable to modern technologies owing to their unique luminescent, chemical, and magnetic properties. They play a central role in sustainable technologies such as batteries, wind turbines, and electric vehicles, while their chemical versatility underpins advanced display systems, high-performance magnets, and catalytic processes. Despite their importance, REEs are notoriously difficult to separate because of their highly similar physicochemical properties. Conventional solvent extraction remains the dominant method, though it requires large volumes of hazardous organophosphate surfactants, consumes significant energy, and often demands ∼100 stages for separation at high purities. To address these challenges, biomolecular strategies have recently emerged as promising alternatives, exploiting or engineering the specificity of metalloproteins and their binding loops to achieve selective REE separation. Lanthanide binding tags (LBTs) are short peptides engineered from calcium-binding motifs of metalloproteins such as calmodulin and adapted through directed screening to achieve selective coordination of lanthanide cations (Ln3+). These peptides exhibit high binding affinity and can differentiate among lanthanides across the series. Recently, these molecules have been repurposed for the selective separation of REEs. Understanding how size selectivity arises at the molecular level, however, remains critical. In this work, we investigate how LBTs achieve size selectivity through structural modulation in response to Ln3+ ionic radius, using a combination of solution-state multi-dimensional NMR spectroscopy and molecular dynamics simulations. We show that while overall binding affinity is primarily governed by strongly coordinating charged residues, selectivity is conferred by the structural rearrangement of weaker binding sites. Notably, the N5 asparagine residue functions as a conformati…
abstract: Rare earth elements (REEs), comprising yttrium, scandium, and the lanthanides, are indispensable to modern technologies owing to their unique luminescent, chemical, and magnetic properties. They play a central role in sustainable technologies such as batteries, wind turbines, and electric vehicles, while their chemical versatility underpins advanced display systems, high-performance magnets, and catalytic processes. Despite their importance, REEs are notoriously difficult to separate because of their highly similar physicochemical properties. Conventional solvent extraction remains the dominant method, though it requires large volumes of hazardous organophosphate surfactants, consumes significant energy, and often demands ∼100 stages for separation at high purities. To address these challenges, biomolecular strategies have recently emerged as promising alternatives, exploiting or engineering the specificity of metalloproteins and their binding loops to achieve selective REE separation. Lanthanide binding tags (LBTs) are short peptides engineered from calcium-binding motifs of metalloproteins such as calmodulin and adapted through directed screening to achieve selective coordination of lanthanide cations (Ln3+). These peptides exhibit high binding affinity and can differentiate among lanthanides across the series. Recently, these molecules have been repurposed for the selective separation of REEs. Understanding how size selectivity arises at the molecular level, however, remains critical. In this work, we investigate how LBTs achieve size selectivity through structural modulation in response to Ln3+ ionic radius, using a combination of solution-state multi-dimensional NMR spectroscopy and molecular dynamics simulations. We show that while overall binding affinity is primarily governed by strongly coordinating charged residues, selectivity is conferred by the structural rearrangement of weaker binding sites. Notably, the N5 asparagine residue functions as a conformati…
author: KT, Surabh
keywords: rare earth elements, bioseparation, peptides, lanthanide binding tags, selectivity, nanoparticles, foam fractionation, Analytical Chemistry, Biochemical and Biomolecular Engineering, Chemical Engineering, Chemistry, Computational Chemistry, Inorganic Chemistry, Other Chemical Engineering, Structural Biology
date published: 2025-01-01T08:00:00Z
date modified: 2026-07-24T01:58:13Z
provider: City University of New York - City College
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: City University of New York - City College