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 Experiment Videos

Functionalized oligoanthranilamides: modular and conformationally controlled scaffolds.

Y Hamuro1, A D Hamilton

  • 1Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.

Bioorganic & Medicinal Chemistry
|September 13, 2001
PubMed
Summary
This summary is machine-generated.

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

Medical professional involvement in smartphone 'apps' in dermatology.

The British journal of dermatology·2012
Same author

Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.

Journal of molecular biology·2009
Same author

Farnesyltransferase and geranylgeranyltransferase I inhibitors upregulate RhoB expression by HDAC1 dissociation, HAT association and histone acetylation of the RhoB promoter.

Oncogene·2006
Same author

Anticancer activity of farnesyltransferase and geranylgeranyltransferase I inhibitors: prospects for drug development.

Expert opinion on investigational drugs·2005
Same author

The farnesyl transferase inhibitor, FTI-277, inhibits growth and induces apoptosis in drug-resistant myeloma tumor cells.

Leukemia·2003
Same author

Disruption of protein-protein interactions: design of a synthetic receptor that blocks the binding of cytochrome c to cytochrome c peroxidase.

Chemical communications (Cambridge, England)·2002

Functionalized oligoanthranilamides serve as stable scaffolds for molecular recognition. These conformationally controlled structures can form hydrogen-bonded complexes with specific peptide substrates.

Area of Science:

  • Supramolecular Chemistry
  • Organic Chemistry
  • Chemical Biology

Background:

  • Developing conformationally controlled scaffolds is crucial for precise molecular recognition.
  • Oligoanthranilamides offer a unique structural motif stabilized by intramolecular hydrogen bonds.
  • Peptide recognition units can be appended to these scaffolds for targeted interactions.

Purpose of the Study:

  • To investigate the utility of functionalized oligoanthranilamides as scaffolds for molecular recognition.
  • To explore the conformational stability and self-assembly properties of these molecules.
  • To demonstrate selective binding of peptide substrates by functionalized scaffolds.

Main Methods:

  • Synthesis of functionalized oligoanthranilamides with di- or tripeptide units.

Related Experiment Videos

  • 1H NMR dilution experiments in CDCl(3) to study self-assembly.
  • Assessment of binding selectivity using specific peptide substrates.

    • Main Results:

    • Oligoanthranilamide strands adopt a stable linear conformation stabilized by intramolecular hydrogen bonds.
    • 1H NMR data indicate the formation of extended hydrogen-bonded sheet dimers.
    • Functionalized strands selectively bind dipeptide substrates, such as hexanoyl alanylalanine, over esters.

    Conclusions:

    • Functionalized oligoanthranilamides provide a modular and stable scaffold for molecular recognition.
    • The conformational control offered by these scaffolds enables specific binding of peptide substrates.
    • This design holds promise for developing advanced molecular recognition systems.