English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating Lipopeptide MALP-2 and of Its Constituent Peptide

Castelletto, V., Kirkham, S., Hamley, I. W., Kowalczyk, R. M., Rabe, M., Reza, M., et al. (2016). Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating Lipopeptide MALP-2 and of Its Constituent Peptide. Biomacromolecules, 17(2), 631-640. doi:10.1021/acs.biomac.5b01573.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0001-B72E-E Version Permalink: http://hdl.handle.net/21.11116/0000-0001-B72F-D
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Castelletto, Valeria1, Author              
Kirkham, Steven1, Author              
Hamley, Ian W.1, Author              
Kowalczyk, Radosław M.1, Author              
Rabe, Martin2, Author              
Reza, Mehedi3, Author              
Ruokolainen, Janne T.3, Author              
Affiliations:
1School of Chemistry, Pharmacy and Food Biosciences, University of Reading, Whiteknights, Reading, UK, persistent22              
2Interface Spectroscopy, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society, ou_1863358              
3Department of Applied Physics, Aalto University, School of Science, P.O. Box 15100, Aalto, Finland, persistent22              

Content

show
hide
Free keywords: Chemical activation; Macrophages; Medical applications; Peptides; Solutions; X ray diffraction; X ray scattering, Biomedical applications; Critical aggregation concentration; Lipopeptides; Molecular packings; Raft structure; Self-assemble; Toll-like receptors; Twisted tapes, Self assembly, macrophage activating lipopeptide 2; lipopeptide; macrophage stimulatory lipopeptide 2; peptide fragment, aqueous solution; Article; beta sheet; chemical structure; morphology; priority journal; protein aggregation; protein assembly; protein motif; protein secondary structure; X ray crystallography; X ray diffraction; amino acid sequence; chemistry; molecular genetics; protein multimerization; small angle scattering, Amino Acid Sequence; Lipopeptides; Molecular Sequence Data; Peptide Fragments; Protein Multimerization; Scattering, Small Angle; X-Ray Diffraction
 Abstract: The self-assembly of the macrophage-activating lipopeptide MALP-2 in aqueous solution has been investigated and is compared to that of the constituent peptide GNNDESNISFKEK. MALP-2 is a toll-like receptor agonist lipopeptide with diverse potential biomedical applications and its self-assembly has not previously been examined. It is found to self-assemble, above a critical aggregation concentration (cac), into remarkable "fibre raft" structures, based on lateral aggregation of β-sheet based bilayer tapes. Peptide GNNDESNISFKEK also forms β-sheet structures above a cac, although the morphology is distinct, comprising highly extended and twisted tape structures. A detailed insight into the molecular packing within the MALP-2 raft and GNNDESNISFKEK nanotape structures is obtained through X-ray diffraction and small-angle X-ray scattering. These results point to the significant influence of the attached lipid chains on the self-assembly motif, which lead to the raft structure for the lipopeptide assemblies. © 2016 American Chemical Society.

Details

show
hide
Language(s): eng - English
 Dates: 2016-02-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/acs.biomac.5b01573
BibTex Citekey: Castelletto2016631
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biomacromolecules
  Other : Biomacromolecules
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 17 (2) Sequence Number: - Start / End Page: 631 - 640 Identifier: ISSN: 1525-7797
CoNE: https://pure.mpg.de/cone/journals/resource/969870273004