Design of 11-residue peptides with unusual biophysical properties:induced secondary structure in the absence of water

Xiaoqun Mo, Yasuaki Hiromasa, Matt Warner, Ahlam N. Al-Rawi, Takeo Iwamoto, Talat S. Rahman, Xiuzhi Sun, John M. Tomich

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

A series of oligopeptides with β-forming and adhesive properties, were synthesized and analyzed for adhesion shear strength, secondary structure, and association properties. The sequences contained related hydrophobic core segments varying in length from 5 to 12 residues and flanked by di- or tri-lysine segments. Three remarkable peptides consisting of just 11 residues with hydrophobic core sequences of FLIVI, IGSII, and IVIGS flanked by three lysine residues gave the highest dry adhesion shear strength and displayed unusual biophysical properties in the presence and absence of water. KKKFLIVIKKK had its highest adhesion strength at 2% (w/v) at pH 12.0 and showed the highest adhesion strength after exposure to water (water resistance). Both KKKIGSIIKKK and KKKIVIGSKKK, at 4% (w/v) at pH 12.0, displayed nearly identical dry shear strength values to that with the FLIVI core sequence. The peptide with IGSII core, however, displayed a lower water resistance and the latter, IVIGS, showed no water resistance, completely delaminating upon soaking in water. These are the smallest peptides with adhesive properties reported to date and show remarkable adhesion strength even at lower concentrations of 0.2% (w/v), which corresponds to 1.6 mM. The FLIVI containing peptide adopted a β-sheet secondary structure in water while the IGSII- and IVIGS-containing sequences folded similarly only in the absence of water. Analytical ultracentrifugation studies showed that when the FLIVI sequence adopts β-structure in aqueous solution, it associates into a large molecular weight assembly. The random coils of IGSII and IVIGS showed no tendency to associate at any pH.

Original languageEnglish
Pages (from-to)1807-1817
Number of pages11
JournalBiophysical Journal
Volume94
Issue number5
DOIs
Publication statusPublished - Mar 1 2008

Fingerprint

Peptides
Water
Shear Strength
Lysine
Adhesives
Oligopeptides
Ultracentrifugation
Molecular Weight

All Science Journal Classification (ASJC) codes

  • Biophysics

Cite this

Design of 11-residue peptides with unusual biophysical properties:induced secondary structure in the absence of water. / Mo, Xiaoqun; Hiromasa, Yasuaki; Warner, Matt; Al-Rawi, Ahlam N.; Iwamoto, Takeo; Rahman, Talat S.; Sun, Xiuzhi; Tomich, John M.

In: Biophysical Journal, Vol. 94, No. 5, 01.03.2008, p. 1807-1817.

Research output: Contribution to journalArticle

Mo, Xiaoqun ; Hiromasa, Yasuaki ; Warner, Matt ; Al-Rawi, Ahlam N. ; Iwamoto, Takeo ; Rahman, Talat S. ; Sun, Xiuzhi ; Tomich, John M. / Design of 11-residue peptides with unusual biophysical properties:induced secondary structure in the absence of water. In: Biophysical Journal. 2008 ; Vol. 94, No. 5. pp. 1807-1817.
@article{1e42892b4d86409c84faaa80a52ac826,
title = "Design of 11-residue peptides with unusual biophysical properties:induced secondary structure in the absence of water",
abstract = "A series of oligopeptides with β-forming and adhesive properties, were synthesized and analyzed for adhesion shear strength, secondary structure, and association properties. The sequences contained related hydrophobic core segments varying in length from 5 to 12 residues and flanked by di- or tri-lysine segments. Three remarkable peptides consisting of just 11 residues with hydrophobic core sequences of FLIVI, IGSII, and IVIGS flanked by three lysine residues gave the highest dry adhesion shear strength and displayed unusual biophysical properties in the presence and absence of water. KKKFLIVIKKK had its highest adhesion strength at 2{\%} (w/v) at pH 12.0 and showed the highest adhesion strength after exposure to water (water resistance). Both KKKIGSIIKKK and KKKIVIGSKKK, at 4{\%} (w/v) at pH 12.0, displayed nearly identical dry shear strength values to that with the FLIVI core sequence. The peptide with IGSII core, however, displayed a lower water resistance and the latter, IVIGS, showed no water resistance, completely delaminating upon soaking in water. These are the smallest peptides with adhesive properties reported to date and show remarkable adhesion strength even at lower concentrations of 0.2{\%} (w/v), which corresponds to 1.6 mM. The FLIVI containing peptide adopted a β-sheet secondary structure in water while the IGSII- and IVIGS-containing sequences folded similarly only in the absence of water. Analytical ultracentrifugation studies showed that when the FLIVI sequence adopts β-structure in aqueous solution, it associates into a large molecular weight assembly. The random coils of IGSII and IVIGS showed no tendency to associate at any pH.",
author = "Xiaoqun Mo and Yasuaki Hiromasa and Matt Warner and Al-Rawi, {Ahlam N.} and Takeo Iwamoto and Rahman, {Talat S.} and Xiuzhi Sun and Tomich, {John M.}",
year = "2008",
month = "3",
day = "1",
doi = "10.1529/biophysj.107.118299",
language = "English",
volume = "94",
pages = "1807--1817",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "5",

}

TY - JOUR

T1 - Design of 11-residue peptides with unusual biophysical properties:induced secondary structure in the absence of water

AU - Mo, Xiaoqun

AU - Hiromasa, Yasuaki

AU - Warner, Matt

AU - Al-Rawi, Ahlam N.

AU - Iwamoto, Takeo

AU - Rahman, Talat S.

AU - Sun, Xiuzhi

AU - Tomich, John M.

PY - 2008/3/1

Y1 - 2008/3/1

N2 - A series of oligopeptides with β-forming and adhesive properties, were synthesized and analyzed for adhesion shear strength, secondary structure, and association properties. The sequences contained related hydrophobic core segments varying in length from 5 to 12 residues and flanked by di- or tri-lysine segments. Three remarkable peptides consisting of just 11 residues with hydrophobic core sequences of FLIVI, IGSII, and IVIGS flanked by three lysine residues gave the highest dry adhesion shear strength and displayed unusual biophysical properties in the presence and absence of water. KKKFLIVIKKK had its highest adhesion strength at 2% (w/v) at pH 12.0 and showed the highest adhesion strength after exposure to water (water resistance). Both KKKIGSIIKKK and KKKIVIGSKKK, at 4% (w/v) at pH 12.0, displayed nearly identical dry shear strength values to that with the FLIVI core sequence. The peptide with IGSII core, however, displayed a lower water resistance and the latter, IVIGS, showed no water resistance, completely delaminating upon soaking in water. These are the smallest peptides with adhesive properties reported to date and show remarkable adhesion strength even at lower concentrations of 0.2% (w/v), which corresponds to 1.6 mM. The FLIVI containing peptide adopted a β-sheet secondary structure in water while the IGSII- and IVIGS-containing sequences folded similarly only in the absence of water. Analytical ultracentrifugation studies showed that when the FLIVI sequence adopts β-structure in aqueous solution, it associates into a large molecular weight assembly. The random coils of IGSII and IVIGS showed no tendency to associate at any pH.

AB - A series of oligopeptides with β-forming and adhesive properties, were synthesized and analyzed for adhesion shear strength, secondary structure, and association properties. The sequences contained related hydrophobic core segments varying in length from 5 to 12 residues and flanked by di- or tri-lysine segments. Three remarkable peptides consisting of just 11 residues with hydrophobic core sequences of FLIVI, IGSII, and IVIGS flanked by three lysine residues gave the highest dry adhesion shear strength and displayed unusual biophysical properties in the presence and absence of water. KKKFLIVIKKK had its highest adhesion strength at 2% (w/v) at pH 12.0 and showed the highest adhesion strength after exposure to water (water resistance). Both KKKIGSIIKKK and KKKIVIGSKKK, at 4% (w/v) at pH 12.0, displayed nearly identical dry shear strength values to that with the FLIVI core sequence. The peptide with IGSII core, however, displayed a lower water resistance and the latter, IVIGS, showed no water resistance, completely delaminating upon soaking in water. These are the smallest peptides with adhesive properties reported to date and show remarkable adhesion strength even at lower concentrations of 0.2% (w/v), which corresponds to 1.6 mM. The FLIVI containing peptide adopted a β-sheet secondary structure in water while the IGSII- and IVIGS-containing sequences folded similarly only in the absence of water. Analytical ultracentrifugation studies showed that when the FLIVI sequence adopts β-structure in aqueous solution, it associates into a large molecular weight assembly. The random coils of IGSII and IVIGS showed no tendency to associate at any pH.

UR - http://www.scopus.com/inward/record.url?scp=41449116056&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=41449116056&partnerID=8YFLogxK

U2 - 10.1529/biophysj.107.118299

DO - 10.1529/biophysj.107.118299

M3 - Article

C2 - 18024497

AN - SCOPUS:41449116056

VL - 94

SP - 1807

EP - 1817

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 5

ER -