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 language | English |
|---|---|
| Pages (from-to) | 212-215 |
| Number of pages | 4 |
| Journal | Journal of the American Chemical Society |
| Volume | 122 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Jan 19 2000 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
Cite this
Design of a heterotrimeric α-helical bundle by hydrophobic core engineering. / Kashiwada, Ayumi; Hiroaki, Hidekazu; Kohda, Daisuke; Nango, Mamoru; Tanaka, Toshiki.
In: Journal of the American Chemical Society, Vol. 122, No. 2, 19.01.2000, p. 212-215.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Design of a heterotrimeric α-helical bundle by hydrophobic core engineering
AU - Kashiwada, Ayumi
AU - Hiroaki, Hidekazu
AU - Kohda, Daisuke
AU - Nango, Mamoru
AU - Tanaka, Toshiki
PY - 2000/1/19
Y1 - 2000/1/19
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033968472&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033968472&partnerID=8YFLogxK
U2 - 10.1021/ja993190q
DO - 10.1021/ja993190q
M3 - Article
AN - SCOPUS:0033968472
VL - 122
SP - 212
EP - 215
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 2
ER -