2016
DOI: 10.1002/cphc.201600670
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Optical Modulation of Azobenzene‐Modified Peptide for Gold Surface Binding

Abstract: The ability to precisely and remotely modulate reversible binding interactions between biomolecules and abiotic surfaces is appealing for many applications. To achieve this level of control, an azobenzene-based optical switch is added to nanoparticle-binding peptides in order to switch peptide conformation and attenuate binding affinity to gold surfaces via binding and dissociation of peptides.

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Cited by 8 publications
(11 citation statements)
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References 40 publications
(100 reference statements)
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“…This approach is not limited to switching by protease activity, described in this study. Substitution of the protease substrate sequence with other enzymatic substrate sequences or artificial moieties such as photo-switching and chemo-switching functional groups could further provide a variety of well-controlled switching nanodevices [ 63 , 64 , 65 , 66 ]. Such systems hold promise for regulating the formation of nanowire structures for various applications, including electronic circuits for use in nanotechnologies and nanobiotechnologies.…”
Section: Discussionmentioning
confidence: 99%
“…This approach is not limited to switching by protease activity, described in this study. Substitution of the protease substrate sequence with other enzymatic substrate sequences or artificial moieties such as photo-switching and chemo-switching functional groups could further provide a variety of well-controlled switching nanodevices [ 63 , 64 , 65 , 66 ]. Such systems hold promise for regulating the formation of nanowire structures for various applications, including electronic circuits for use in nanotechnologies and nanobiotechnologies.…”
Section: Discussionmentioning
confidence: 99%
“…These changes in the isomerization state alter the affinity of the biomolecule for the metallic surface and can be used to optically tune the final size of the NP. 21,22 Photoisomerization can also be accomplished using nonlinear optical approaches under specific conditions. 21 The catalytic properties of NPs capped with photoswitchable peptides are sensitive to isomerization-based structural changes and can be varied between two different reaction regimes based upon the reversible peptide conformation.…”
Section: ■ Introductionmentioning
confidence: 99%
“…As an alternative to conventional ligands, one can employ materials directing peptides that recognize, bind, and stabilize colloidal dispersions of NPs. ,, These peptides have a strong affinity for inorganic surfaces through the multiple, weak noncovalent interactions of the individual residues, which can be manipulated to change the peptide surface conformation. , One approach to triggering peptide conformational changes is via optical stimulation. , Through conjugation of a non-natural azobenzene photoswitch into the peptides, reversible changes in the biomolecular overlayer structure on a NP surface can be accessed via azobenzene photoisomerization (e.g. cis vs trans).…”
Section: Introductionmentioning
confidence: 99%
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“…Such inorganic materialsmade by laboratory evolved or engineered biomolecules (peptides, proteins, nucleic acids) attract attention for catalysis, self-assembly, and in bio-contrast (labeling) applications. [4][5][6][7][8] Any self-contained biological system for synthesizing an inorganic nanostructure will generally require an oxidoreductase activity, enabling conversion of inorganic ions from soluble to insoluble oxidation states. Ferritins and DPS proteins accomplish this with ferroxidase enzymatic centers.…”
mentioning
confidence: 99%