2015
DOI: 10.1021/jacs.5b04285
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Protein-Induced Supramolecular Disassembly of Amphiphilic Polypeptide Nanoassemblies

Abstract: Mimicking non-covalent interaction based processes in nature has been an important goal of supramolecular chemistry. Here, we report on amphiphilic polypeptides that self-assemble to form nanoscale supramolecular assemblies and are programmed to disassemble in response to a specific protein. Benzenesulfonamide and carbonic anhydrase have been chosen as the ligand and protein respectively to demonstrate this possibility. Since the amphiphilic nanoassembly sequesters hydrophobic guest molecules, the protein-spec… Show more

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Cited by 85 publications
(59 citation statements)
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“…377 Another study also described protein responsive-amphiphilic polypeptide nanoassemblies that disassembled when a particular protein bound to the nanostructure with potential applications in protein-specific delivery and diagnostics. 378 …”
Section: Different Stimuli-responsive Mnpsmentioning
confidence: 99%
“…377 Another study also described protein responsive-amphiphilic polypeptide nanoassemblies that disassembled when a particular protein bound to the nanostructure with potential applications in protein-specific delivery and diagnostics. 378 …”
Section: Different Stimuli-responsive Mnpsmentioning
confidence: 99%
“…5A). 31 Driven by hydrophobic forces, the benzenesulfonamide containing polypeptide P10 self-assembles to form spherical nanoparticles as shown in Fig. 5B.…”
Section: Disassemblymentioning
confidence: 99%
“…This technique is capable of nanoscale particle hydrodynamic radius (R H ) measurements in solution and is suitable for peptide/protein assays (38). The number-averaged size distribution profiles of each peptide were used to retrieve the modal R H at different peptide concentrations (Fig.…”
Section: Lipid-conjugated Inhibitory Peptides Self-assemble Into Nanomentioning
confidence: 99%