Design of a heterotrimeric α-helical bundle by hydrophobic core engineering

Ayumi Kashiwada, Hidekazu Hiroaki, Daisuke Kohda, Mamoru Nango, Toshiki Tanaka

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

We previously prepared the de novo designed peptide, [YGG(IEKKIEA)4], which forms a parallel triple-stranded coiled coil. To prepare an AAB-type heterotrimeric α-helical bundle, two variants, where the Ile15 residue in the hydrophobic position was replaced with either an Ala or Trp residue, were designed and named IZ-2A and IZ-2W, respectively. Circular dichroism spectroscopy, peptide titration, sedimentation equilibrium, and gel filtration analyses revealed the formation of an (IZ-2A)2/IZ-2W complex. The NOESY spectra analyses indicated the presence of interstrand interactions between the two Ala residues and the Trp residue in the hydrophobic core. The (IZ-2A)2/IZ-2W complex has the structural uniqueness of native proteins.

Original languageEnglish
Pages (from-to)212-215
Number of pages4
JournalJournal of the American Chemical Society
Volume122
Issue number2
DOIs
Publication statusPublished - Jan 19 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Design of a heterotrimeric α-helical bundle by hydrophobic core engineering'. Together they form a unique fingerprint.

Cite this