Role of positions e and g in the fibrous assembly formation of an amphipathic α-helix-forming polypeptide

Toshiaki Takei, Kouhei Tsumoto, Masakuni Yoshino, Shuichi Kojima, Kazumori Yazaki, Takuya Ueda, Tsunetomo Takei, Fumio Arisaka, Kin Ichiro Miura

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

We previously characterized α3, a polypeptide that has a three times repeated sequence of seven amino acids (abcdefg: LETLAKA) and forms fibrous assemblies composed of amphipathic a-helices. Upon comparison of the amino acid sequences of α3 with other a-helix forming polypeptides, we proposed that the fibrous assemblies were formed due to the alanine (Ala) residues at positions e and g. Here, we characterized seven α3 analog polypeptides with serine (Ser), glycine (Gly), or charged residues substituted for Ala at positions e and g. The α-helix forming abilities of the substituted polypeptides were less than that of α3. The polypeptides with amino acid substitutions at position g and the polypeptide KEα3, in which Ala was substituted with charged amino acids, formed few fibrous assemblies. In contrast, polypeptides with Ala replaced by Ser at position e formed β-sheets under several conditions. These results show that Ala residues at position e and particularly at position g are involved in the formation of fibrous assemblies.

Original languageEnglish
Pages (from-to)260-272
Number of pages13
JournalBiopolymers - Peptide Science Section
Volume102
Issue number3
DOIs
Publication statusPublished - 2014 May 1
Externally publishedYes

Fingerprint

Polypeptides
Alanine
Amino acids
Peptides
Amino Acids
Serine
Amino Acid Sequence
Amino Acid Substitution
Glycine
Substitution reactions

Keywords

  • Aggregation
  • Amphipathic α-helix
  • Fibrous assembly
  • Self-assembly

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Role of positions e and g in the fibrous assembly formation of an amphipathic α-helix-forming polypeptide. / Takei, Toshiaki; Tsumoto, Kouhei; Yoshino, Masakuni; Kojima, Shuichi; Yazaki, Kazumori; Ueda, Takuya; Takei, Tsunetomo; Arisaka, Fumio; Miura, Kin Ichiro.

In: Biopolymers - Peptide Science Section, Vol. 102, No. 3, 01.05.2014, p. 260-272.

Research output: Contribution to journalArticle

Takei, T, Tsumoto, K, Yoshino, M, Kojima, S, Yazaki, K, Ueda, T, Takei, T, Arisaka, F & Miura, KI 2014, 'Role of positions e and g in the fibrous assembly formation of an amphipathic α-helix-forming polypeptide', Biopolymers - Peptide Science Section, vol. 102, no. 3, pp. 260-272. https://doi.org/10.1002/bip.22479
Takei, Toshiaki ; Tsumoto, Kouhei ; Yoshino, Masakuni ; Kojima, Shuichi ; Yazaki, Kazumori ; Ueda, Takuya ; Takei, Tsunetomo ; Arisaka, Fumio ; Miura, Kin Ichiro. / Role of positions e and g in the fibrous assembly formation of an amphipathic α-helix-forming polypeptide. In: Biopolymers - Peptide Science Section. 2014 ; Vol. 102, No. 3. pp. 260-272.
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