Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Reprogramming Chirality in Peptide Self-Assembly via Intramolecular Side Chain-Backbone Hydrogen Bonding.

Nano letters·2026
Same author

Realising the full potential of biocides in the fight against antimicrobial resistance.

Expert opinion on drug discovery·2026
Same author

Selective Serine Substitutions of Antimicrobial Peptides Reveal Different Mechanistic Actions Toward Gram-Negative Bacteria.

ACS applied materials & interfaces·2026
Same author

Short Arg- and Trp-Rich Lipopeptides Kill Resistant Bacterial Pathogens via Effective Membrane Disruption.

Biomacromolecules·2026
Same author

Rational Design of Broad-Spectrum Antimicrobial Peptides Derived from the Dengue Virus Capsid Alpha2 Sequence.

ACS applied materials & interfaces·2025
Same author

Microrheology of Monoclonal Antibodies during Gelation under Low pH Conditions.

Molecular pharmaceutics·2025

Related Experiment Video

Updated: Jul 7, 2026

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores
09:43

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores

Published on: October 31, 2013

Interfacial nano-structuring of designed peptides regulated by solution pH.

Jian R Lu1, Shiamalee Perumal, Ian Hopkinson

  • 1Biological Physics Group, Department of Physics, UMIST, PO Box 88, Manchester M60 1QD, United Kingdom. j.lu@umist.ac.uk

Journal of the American Chemical Society
|July 22, 2004
PubMed
Summary

Researchers studied how synthetic peptides form layers on silicon oxide. The tryptophan-containing peptide (WWW15) strongly adsorbs, forming a unique helical structure, unlike the tyrosine-containing peptide (YYY15).

More Related Videos

Creating Sub-50 Nm Nanofluidic Junctions in PDMS Microfluidic Chip via Self-Assembly Process of Colloidal Particles
11:13

Creating Sub-50 Nm Nanofluidic Junctions in PDMS Microfluidic Chip via Self-Assembly Process of Colloidal Particles

Published on: March 13, 2016

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone
08:06

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone

Published on: February 23, 2017

Related Experiment Videos

Last Updated: Jul 7, 2026

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores
09:43

Fine-tuning the Size and Minimizing the Noise of Solid-state Nanopores

Published on: October 31, 2013

Creating Sub-50 Nm Nanofluidic Junctions in PDMS Microfluidic Chip via Self-Assembly Process of Colloidal Particles
11:13

Creating Sub-50 Nm Nanofluidic Junctions in PDMS Microfluidic Chip via Self-Assembly Process of Colloidal Particles

Published on: March 13, 2016

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone
08:06

Merging Ion Concentration Polarization between Juxtaposed Ion Exchange Membranes to Block the Propagation of the Polarization Zone

Published on: February 23, 2017

Area of Science:

  • Biophysics
  • Materials Science
  • Surface Chemistry

Background:

  • Understanding peptide adsorption at interfaces is crucial for biomaterials and nanotechnology.
  • The HAP2 protein domain from yeast Saccharomyces cerevisiae provides a basis for synthetic peptide design.
  • Previous studies lack detailed in-situ structural analysis of peptide layers at the solid-liquid interface.

Purpose of the Study:

  • To determine the in-situ conformations of peptide layers formed by synthetic YYY15 and WWW15 peptides.
  • To investigate the effect of pH on peptide adsorption and layer structure at the silicon oxide/aqueous solution interface.
  • To assess the reversibility of peptide adsorption and explore potential applications in nano-templating.

Main Methods:

  • Neutron reflectivity (NR) was employed to analyze the structure of peptide layers at the hydrophilic silicon oxide/aqueous solution interface.
  • Deuterium oxide (D2O) was used as a solvent in NR experiments to enhance contrast and reveal structural heterogeneity.
  • Circular dichroism (CD) spectra were used to confirm the alpha-helical structure of the peptides in phosphate buffer.

Main Results:

  • At pH 7, YYY15 formed a weakly adsorbed monolayer, while WWW15 exhibited strong adsorption with a distinct three-sublayer structure, suggesting a 'sideways-on' helical conformation.
  • Increasing pH to 9 improved packing of the WWW15 layer, while decreasing pH to 5 reduced adsorption due to increased peptide solubility.
  • Adsorbed peptide layers were found to be irreversible, with no significant desorption observed.

Conclusions:

  • The study elucidates the distinct adsorption behaviors and in-situ conformations of YYY15 and WWW15 peptides.
  • The 'sideways-on' helical structure of WWW15 at the interface offers a novel self-assembled architecture.
  • These findings suggest potential applications of such peptide layers in interfacial nano-templating strategies.