A theoretical comparison of self-assembling α- and β-peptide nanostructures

Toward design of β-barrel frameworks

Tamás Beke, András Czajlik, Balázs Bálint, A. Perczel

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Self-assembling peptide-based nanotubes are among the most investigated bioactive compounds as a result of their numerous potential applications as novel biomaterials. To support rational bottom-up design of such artificial nanosystems, here we investigate structural and energetic properties of various sheet-derived nanotubes. We carried out high level quantum chemical calculations on large models, composed of up to 32 amino acids, and characterized structures from extended β-sheets to the molecular framework of β-barrel proteins. Surprisingly, enzyme-resistant nonnatural β-peptides have an affinity to form nanotubes that is remarkably higher than that of natural α-peptides. We analyzed the stability of both systems depending on (i) parallel or antiparallel orientation, (ii) the number of peptide strands, and (iii) the formed hydrogen bond pattern. Applicability is outlined by investigating guest molecules in the tubes. It is hoped that the structural and energetic data presented here will be effectively used in the design of novel peptide nanosystems.

Original languageEnglish
Pages (from-to)545-553
Number of pages9
JournalACS Nano
Volume2
Issue number3
DOIs
Publication statusPublished - Mar 2008

Fingerprint

assembling
Peptides
peptides
Nanostructures
Nanotubes
Nanosystems
nanotubes
Biocompatible Materials
activity (biology)
Biomaterials
strands
amino acids
affinity
Amino acids
enzymes
Hydrogen bonds
Enzymes
hydrogen bonds
tubes
proteins

Keywords

  • β-barrel
  • β-sheet
  • Ab initio
  • DFT
  • Nanotube
  • Peptide
  • Self-assembly

ASJC Scopus subject areas

  • Engineering(all)
  • Materials Science(all)
  • Physics and Astronomy(all)

Cite this

A theoretical comparison of self-assembling α- and β-peptide nanostructures : Toward design of β-barrel frameworks. / Beke, Tamás; Czajlik, András; Bálint, Balázs; Perczel, A.

In: ACS Nano, Vol. 2, No. 3, 03.2008, p. 545-553.

Research output: Contribution to journalArticle

Beke, Tamás ; Czajlik, András ; Bálint, Balázs ; Perczel, A. / A theoretical comparison of self-assembling α- and β-peptide nanostructures : Toward design of β-barrel frameworks. In: ACS Nano. 2008 ; Vol. 2, No. 3. pp. 545-553.
@article{b2b1738c11484ed3a728d0787a182982,
title = "A theoretical comparison of self-assembling α- and β-peptide nanostructures: Toward design of β-barrel frameworks",
abstract = "Self-assembling peptide-based nanotubes are among the most investigated bioactive compounds as a result of their numerous potential applications as novel biomaterials. To support rational bottom-up design of such artificial nanosystems, here we investigate structural and energetic properties of various sheet-derived nanotubes. We carried out high level quantum chemical calculations on large models, composed of up to 32 amino acids, and characterized structures from extended β-sheets to the molecular framework of β-barrel proteins. Surprisingly, enzyme-resistant nonnatural β-peptides have an affinity to form nanotubes that is remarkably higher than that of natural α-peptides. We analyzed the stability of both systems depending on (i) parallel or antiparallel orientation, (ii) the number of peptide strands, and (iii) the formed hydrogen bond pattern. Applicability is outlined by investigating guest molecules in the tubes. It is hoped that the structural and energetic data presented here will be effectively used in the design of novel peptide nanosystems.",
keywords = "β-barrel, β-sheet, Ab initio, DFT, Nanotube, Peptide, Self-assembly",
author = "Tam{\'a}s Beke and Andr{\'a}s Czajlik and Bal{\'a}zs B{\'a}lint and A. Perczel",
year = "2008",
month = "3",
doi = "10.1021/nn700252s",
language = "English",
volume = "2",
pages = "545--553",
journal = "ACS Nano",
issn = "1936-0851",
publisher = "American Chemical Society",
number = "3",

}

TY - JOUR

T1 - A theoretical comparison of self-assembling α- and β-peptide nanostructures

T2 - Toward design of β-barrel frameworks

AU - Beke, Tamás

AU - Czajlik, András

AU - Bálint, Balázs

AU - Perczel, A.

PY - 2008/3

Y1 - 2008/3

N2 - Self-assembling peptide-based nanotubes are among the most investigated bioactive compounds as a result of their numerous potential applications as novel biomaterials. To support rational bottom-up design of such artificial nanosystems, here we investigate structural and energetic properties of various sheet-derived nanotubes. We carried out high level quantum chemical calculations on large models, composed of up to 32 amino acids, and characterized structures from extended β-sheets to the molecular framework of β-barrel proteins. Surprisingly, enzyme-resistant nonnatural β-peptides have an affinity to form nanotubes that is remarkably higher than that of natural α-peptides. We analyzed the stability of both systems depending on (i) parallel or antiparallel orientation, (ii) the number of peptide strands, and (iii) the formed hydrogen bond pattern. Applicability is outlined by investigating guest molecules in the tubes. It is hoped that the structural and energetic data presented here will be effectively used in the design of novel peptide nanosystems.

AB - Self-assembling peptide-based nanotubes are among the most investigated bioactive compounds as a result of their numerous potential applications as novel biomaterials. To support rational bottom-up design of such artificial nanosystems, here we investigate structural and energetic properties of various sheet-derived nanotubes. We carried out high level quantum chemical calculations on large models, composed of up to 32 amino acids, and characterized structures from extended β-sheets to the molecular framework of β-barrel proteins. Surprisingly, enzyme-resistant nonnatural β-peptides have an affinity to form nanotubes that is remarkably higher than that of natural α-peptides. We analyzed the stability of both systems depending on (i) parallel or antiparallel orientation, (ii) the number of peptide strands, and (iii) the formed hydrogen bond pattern. Applicability is outlined by investigating guest molecules in the tubes. It is hoped that the structural and energetic data presented here will be effectively used in the design of novel peptide nanosystems.

KW - β-barrel

KW - β-sheet

KW - Ab initio

KW - DFT

KW - Nanotube

KW - Peptide

KW - Self-assembly

UR - http://www.scopus.com/inward/record.url?scp=45149135447&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=45149135447&partnerID=8YFLogxK

U2 - 10.1021/nn700252s

DO - 10.1021/nn700252s

M3 - Article

VL - 2

SP - 545

EP - 553

JO - ACS Nano

JF - ACS Nano

SN - 1936-0851

IS - 3

ER -