Tracing chirality, diameter dependence, and temperature-controlling of single-walled carbon nanotube non-covalent functionalization by biologically compatible peptide: insights from molecular dynamics simulations

Tohidifar, Leila; Hadipour, Nasser L.

doi:10.1007/s00894-019-4154-9

Cited by 4 publications

(1 citation statement)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We hypothesized that the ability to disperse SWNTs in aqueous media was related to the affinity of the peptide to the nanotube surface. The extreme surface area and cohesive energy between adjacent SWNTs naturally drives the tubes to form strong aggregates in commercially obtained nanotubes thus causing difficulty in aqueous dispersion [29]. SWNTs are incompatible with polar aprotic solvents which make the downstream processing of the tubes much more challenging than other conventional materials [9,30].…”

Section: Peptide Cnt Dispersion: Binding Characterizationmentioning

confidence: 99%

Identification of Chiral-Specific Carbon Nanotube Binding Peptides Using a Modified Biopanning Method

et al. 2021

View full text Add to dashboard Cite

Peptides can recognize and selectively bind to a wide variety of materials dependent on both their surface properties and the environment. Biopanning with phage or cell peptide display libraries can identify material-specific binding peptides. However, the limitations with sequence diversity of traditional bacteriophage (phage) display libraries and loss of unique phage clones during the amplification cycles results in a smaller pool of peptide sequences identified. False positive sequences tend to emerge during the biopanning process due to highly proliferating, yet nonspecific, phages. In order to overcome this limitation of traditional biopanning methodology, a modified method using high-throughput next generation sequencing (HTS) was tested to select for unique peptides specific to two types of single wall carbon nanotube (SWNTs) sources with varying diameter distribution and chirality. Here, the process, analysis, and characterization of peptide sequences identified using the modified method is further described and compared to a peptide identified in literature using the traditional method. Selected sequences from this study were incorporated in a SWNT dispersion experiment to probe their selectivity to the nanotube diameter. We show that NHTS can uncover unique binding sequences that might have otherwise been lost during the traditional biopanning method.

show abstract

Section: Peptide Cnt Dispersion: Binding Characterizationmentioning

confidence: 99%