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

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

doi:10.1021/ja993190q

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 journal › Article › peer-review

45 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 language	English
Pages (from-to)	212-215
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	122
Issue number	2
DOIs	https://doi.org/10.1021/ja993190q
Publication status	Published - Jan 19 2000
Externally published	Yes

All Science Journal Classification (ASJC) codes

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja993190q

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title = "Design of a heterotrimeric α-helical bundle by hydrophobic core engineering",

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.",

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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

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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.

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

Abstract

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