Recognition of poly(dimethylsiloxane) with phage displayed peptides

Swaminathan, Swathi; Cui, Yue

doi:10.1039/c2ra22137c

Cited by 11 publications

(14 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Also, the peptide NERALTL appeared twice in the database, with binding activity to epoxy covered surfaces [ 38 ] and to the fusion protein of the infectious salmon anemia virus [ 39 ]. Additionally, the peptide LSNNNLR was previously reported to bind poly(dimethylsiloxane) [ 40 ].…”

Section: Resultsmentioning

confidence: 99%

Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2

Guardia

Quijada

Lleonart

2017

Advances in Virology

View full text Add to dashboard Cite

Dengue virus is a growing public health threat that affects hundreds of million peoples every year and leave huge economic and social damage. The virus is transmitted by mosquitoes and the incidence of the disease is increasing, among other causes, due to the geographical expansion of the vector's range and the lack of effectiveness in public health interventions in most prevalent countries. So far, no highly effective vaccine or antiviral has been developed for this virus. Here we employed phage display technology to identify peptides able to block the DENV2. A random peptide library presented in M13 phages was screened with recombinant dengue envelope and its fragment domain III. After four rounds of panning, several binding peptides were identified, synthesized, and tested against the virus. Three peptides were able to block the infectivity of the virus while not being toxic to the target cells. Blind docking simulations were done to investigate the possible mode of binding, showing that all peptides appear to bind domain III of the protein and may be mostly stabilized by hydrophobic interactions. These results are relevant to the development of novel therapeutics against this important virus.

show abstract

Section: Resultsmentioning

confidence: 99%

Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2

Guardia

Quijada

Lleonart

2017

Advances in Virology

View full text Add to dashboard Cite

show abstract

“…As shown in figure 1a, a PDMS film was stretched with a uniaxial stretching strain and subjected to plasma oxidation to generate a hard silica layer on its surface (figure 1a, step 1), followed by releasing the strain form wrinkle patterns (figure 1a, step 2). Recently, we identified specific PDMS-binding phage-displayed peptides (LSNNNLR) with phage display bioscreening [14]. Bringing the wrinkled PDMS surface into contact with a glass substrate coated with PDMS-binding phage-displayed peptides resulted in the patterning of phage-displayed peptides on the crests of the wrinkles ( figure 1a, step 3).…”

Section: Resultsmentioning

confidence: 99%

“…After the final round of panning, DNA sequence analysis yielded heptameric or dodecameric graphene-binding peptides. The PDMSbinding phage-displayed peptide (LSNNNLR) was identified and isolated using the 7-mer phage-displayed kit [14].…”

Section: Screening Of Phage-displayed Peptidesmentioning

confidence: 99%

Non-lithographic patterning of phage-displayed peptides with wrinkled elastomers

Swaminathan

Bullough

et al. 2014

J. R. Soc. Interface.

Self Cite

View full text Add to dashboard Cite

The development of controlled patterning of phage (viruses) could expand opportunities for both fundamental studies and creating various materials platforms. Inducing the elastomeric instability of PDMS film provides a nonlithographic, tuneable, controlled method for generating micro/nanoscale wrinkle patterns. Phage display has emerged as a powerful method for selecting peptides that possess enhanced selectivity and binding affinity toward a variety of targets. In this report, we demonstrate the non-lithographic patterning of phage-displayed peptides with wrinkled elastomers. Our results show that the phage-displayed peptides can be patterned on specific locations in controlled and tuneable ways, be transferred to other substrates and induce the self-assembly of hybrid materials. We anticipate that these results could open up exciting opportunities in fundamental studies and in applications ranging from sensors, hybrid materials, self-assembly, surface and interface, to micro/nanoelectronics.

show abstract

“…Swaminathan and Cui created PDMS microfluidic channels using printed PS as the master mold (as established by Grimes et al) and used these channels to identify specific peptide binding motifs to PDMS via phage display technology. 104 This technology has allowed for the development of bifunctional peptides for the binding of other materials to PDMS, such as streptavidin. Chakraborty et al also leveraged the strainrecovery properties of the heat-shrinkable PS to create superhydrohobic channels.…”

Section: Device Componentsmentioning

confidence: 99%

Thermally-induced miniaturization for micro- and nanofabrication: progress and updates

et al. 2014

View full text Add to dashboard Cite

The field of micro- and nanofabrication has developed extensively in the past several decades with rising interest in alternative fabrication techniques. Growth of these areas has been driven by needs that remain unaddressed by traditional lithographical methods: inexpensive, upscalable, biocompatible, and easily integrated into complete lab-on-a-chip (LOC) systems. Shape memory polymers (SMPs) have been explored as an alternative substrate. This review first focuses on structure fabrication at the micron and nanoscale using specifically heat-shrinkable SMPs and highlights the innovative improvements to this technology in the past several years. The second part of the review illustrates demonstrated applications of these micro- and nanostructures fabricated from heat-shrinkable SMP films. The review concludes with a discussion about future prospects of heat-shrinkable SMP structures for integration into LOC systems.

show abstract

Recognition of poly(dimethylsiloxane) with phage displayed peptides

Cited by 11 publications

References 30 publications

Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2

Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2

Non-lithographic patterning of phage-displayed peptides with wrinkled elastomers

Thermally-induced miniaturization for micro- and nanofabrication: progress and updates

Contact Info

Product

Resources

About