Optical Modulation of Azobenzene‐Modified Peptide for Gold Surface Binding

Kuang, Zhen‐Bang; Knecht, Marc R.; Naik, Rajesh R.

doi:10.1002/cphc.201600670

Cited by 8 publications

(11 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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%

DNA G-Wire Formation Using an Artificial Peptide is Controlled by Protease Activity

et al. 2017

View full text Add to dashboard Cite

The development of a switching system for guanine nanowire (G-wire) formation by external signals is important for nanobiotechnological applications. Here, we demonstrate a DNA nanostructural switch (G-wire <--> particles) using a designed peptide and a protease. The peptide consists of a PNA sequence for inducing DNA to form DNA–PNA hybrid G-quadruplex structures, and a protease substrate sequence acting as a switching module that is dependent on the activity of a particular protease. Micro-scale analyses via TEM and AFM showed that G-rich DNA alone forms G-wires in the presence of Ca2+, and that the peptide disrupted this formation, resulting in the formation of particles. The addition of the protease and digestion of the peptide regenerated the G-wires. Macro-scale analyses by DLS, zeta potential, CD, and gel filtration were in agreement with the microscopic observations. These results imply that the secondary structure change (DNA G-quadruplex <--> DNA/PNA hybrid structure) induces a change in the well-formed nanostructure (G-wire <--> particles). Our findings demonstrate a control system for forming DNA G-wire structures dependent on protease activity using designed peptides. Such systems hold promise for regulating the formation of nanowire for various applications, including electronic circuits for use in nanobiotechnologies.

show abstract

Section: Discussionmentioning

confidence: 99%

DNA G-Wire Formation Using an Artificial Peptide is Controlled by Protease Activity

et al. 2017

View full text Add to dashboard Cite

show abstract

“…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%

“…cis vs trans). 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. , Photoisomerization can also be accomplished using nonlinear optical approaches under specific conditions . 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. , Further studies have demonstrated that additional factors such as the peptide sequence and photoswitch position are critical in determining catalytic activity changes as a function of the peptide overlayer morphology for Au NPs …”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optical Control of Biomimetic Nanoparticle Catalysts Based upon the Metal Component

et al. 2018

Self Cite

View full text Add to dashboard Cite

Nanoparticle catalysts provide an intriguing route to achieving sustainable reactivity. Recent evidence has suggested that both the underlying metallic core and the passivating ligand layer can be exploited to control reactivity. The intimate interactions between the core metal and structure of the ligand layer can change based upon the metal used to generate the catalytic particle. Through judicious selection of both components, nanoparticle catalytic systems can be designed to be stimuli responsive for controlled reactivity. Herein, we demonstrate the effects of the underlying metal on the optically modulated catalytic activity of peptide-capped noble metal nanoparticles. For this, a photoswitch was incorporated into the peptide that enables reversible reconfiguration of the bioligand overlayer structure between two conformations based upon the isomerization state of the photoswitch. These changes in activity are dependent upon the inorganic metal of the particle core, and we exploit this dependence to demonstrate changes in the activity. The materials were fully characterized via spectroscopic methods and microscopy to correlate the observed reactivity to the material composition. The results provide new pathways to achieve remotely responsive catalysts that could be important for controlled multistep reactions or be exploited for other applications including biosensing and plasmonic devices.

show abstract

“…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%

The Metalloid Reductase of Pseudomonas Moravenis Stanleyae Conveys Nanoparticle Mediated Metalloid Tolerance

Nemeth¹,

Neubert²,

Ni³

et al. 2018

Preprint

View full text Add to dashboard Cite

In the present work we have identified a glutathione reductase like metalloid reductase (GRLMR) responsible for mediating selenite tolerance in Pseudomonas moravenis stanleyae through the enzymatic generation of Se(0) nanoparticles. This enzyme has an unprecedented substrate specificity for selenodiglutathione (Km= 336 μM) over oxidized glutathione (Km=8.22 mM). This enzyme was able to induce selenite tolerance in foreign bacterial cell lines by increasing the IC90 for selenite from 1.9 mM in cell lacking the GRLMR gene to 21.3 mM for cells containing the GRLMR gene. It was later confirmed by STEM and EDS that Se nanoparticles were absent in control cells and present in cells expressing GRLMR. Structural analysis suggests the lack of a sulfur residue in the substrate/product binding pocket may be responsible for this unique substrate specificity.

show abstract

Optical Modulation of Azobenzene‐Modified Peptide for Gold Surface Binding

Cited by 8 publications

References 40 publications

DNA G-Wire Formation Using an Artificial Peptide is Controlled by Protease Activity

DNA G-Wire Formation Using an Artificial Peptide is Controlled by Protease Activity

Optical Control of Biomimetic Nanoparticle Catalysts Based upon the Metal Component

The Metalloid Reductase of Pseudomonas Moravenis Stanleyae Conveys Nanoparticle Mediated Metalloid Tolerance

Contact Info

Product

Resources

About