Dataset Information

Protein and enzyme gated supramolecular disassembly.

ABSTRACT: An amphiphilic nanoassembly was designed to respond to the concurrent presence of a protein and an enzyme. We present herein a system, where in the presence of these two stimuli supramolecular disassembly and molecular release occur. This molecular release arises in the form a fluorescence response that has been shown to be specific. We also show that this system can be modified to respond only if light stimulus is also present in addition to the protein and the enzyme. Demonstration of such supramolecular disassembly principles could have broad implications in a variety of biological applications.

SUBMITTER: Guo J

PROVIDER: S-EPMC3985736 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Protein and enzyme gated supramolecular disassembly.

Guo Jing J Zhuang Jiaming J Wang Feng F Raghupathi Krishna R KR Thayumanavan S S

Journal of the American Chemical Society 20140129 6

An amphiphilic nanoassembly was designed to respond to the concurrent presence of a protein and an enzyme. We present herein a system, where in the presence of these two stimuli supramolecular disassembly and molecular release occur. This molecular release arises in the form a fluorescence response that has been shown to be specific. We also show that this system can be modified to respond only if light stimulus is also present in addition to the protein and the enzyme. Demonstration of such sup ...[more]

PMID: 24447098

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Project description:CONSPECTUS: Supramolecular assemblies formed from spontaneous self-assembly of amphiphilic macromolecules are explored as biomimetic architectures and for applications in areas such as sensing, drug delivery, and diagnostics. Macromolecular assemblies are usually preferred, compared with their simpler small molecule counterparts, due to their low critical aggregate concentrations (CAC) and high thermodynamic stability. This Account focuses on the structural and functional aspects of assemblies formed from dendrimers, specifically facially amphiphilic dendrons that form micelle or inverse micelle type supramolecular assemblies depending on the nature of the solvent medium. The micelle type assemblies formed from facially amphiphilic dendrons sequester hydrophobic guest molecules in their interiors. The stability of these assemblies is dependent on the relative compatibility of the hydrophilic and hydrophobic functionalities with water, often referred to as hydrophilic-lipophilic balance (HLB). Disruption of the HLB, using an external stimulus, could lead to disassembly of the aggregates, which can then be utilized to cause an actuation event, such as guest molecule release. Studying these possibilities has led to (i) a robust and general strategy for stimulus-induced disassembly and molecular release and (ii) the introduction of a new approach to protein-responsive supramolecular disassembly. The latter strategy provides a particularly novel avenue for impacting biomedical applications. Most of the stimuli-sensitive supramolecular assemblies have been designed to be responsive to factors such pH, temperature, and redox conditions. The reason for this interest stems from the fact that certain disease microenvironments have aberrations in these factors. However, these variations are the secondary imbalances in biology. Imbalances in protein activity are the primary reasons for most, if not all, human pathology. There have been no robust strategies in stimulus-responsive assemblies that respond to these variations. The facially amphiphilic dendrimers provide a unique opportunity to explore this possibility. Similarly, the propensity of these molecules to form inverse micelles in apolar solvents and thus bind polar guest molecules, combined with the fact that these assemblies do not thermodynamically equilibrate in biphasic mixtures, was used to predictably simplify peptide mixtures. The structure-property relationships developed from these studies have led to a selective and highly sensitive detection of peptides in complex mixtures. Selectivity in peptide extraction was achieved using charge complementarity between the peptides and the hydrophilic components present in inverse micellar interiors. These findings will have implications in areas such as proteomics and biomarker detection.

Dataset Information

Protein and enzyme gated supramolecular disassembly.

Publications

Protein and enzyme gated supramolecular disassembly.

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