NDLI: Hierarchical self-assembly of Tjernberg peptide at nanoscale

Content Provider	Royal Society of Chemistry (RSC)
Author	Krishnan, Uma Maheswari Sethuraman, Swaminathan Kumaraswamy, Priyadharshini
Copyright Year	2013
Abstract	Molecular self-assembly of biomolecules, especially proteins and peptides has elucidated much interest in recent years due to the reproducibility of structures and the high degree of control on the formation kinetics and morphology by varying the self-assembling conditions. These self-assembled structures have found widespread applications in tissue engineering, drug delivery and electronics. Two pentapeptides, namely Soto peptide (LPFFD) and the Tjernberg peptide (KLVFF), have been proposed to effectively curtail amyloid plaque deposits. Being amphipathic, these molecules can undergo self-assembly that can be influenced by a host of factors including concentration, pH, proteins, salt content, etc. However, this facet is scarcely explored till date, which might pave way for the novel treatment strategy for Alzheimer's disease. Our data show that the peptide spontaneously forms micelles and they are rich in beta sheet structures, which is confirmed using FT-IR, SAED and thioflavin binding studies. While, acidic pH seems to have no role in the formation of higher order structures, alkaline pH promotes longitudinal and lateral stacking interactions resulting in formation of higher order structures. We also found that the hydrophobicity and hydrophilicity of the substrate also play a major role in the formation of higher order structures. Moreover, the micelles formed by the KLVFF peptide under various environmental conditions exhibits excellent surface tension lowering effects which is in good agreement with the cell proliferation data that showed the protective ability of KLVFF peptide against Aβ1–42 cytotoxicity indicating its potential in Alzheimer's disease therapy as an aggregation blocking agent.
Starting Page	2684
Ending Page	2694
Page Count	11
File Format	HTM / HTML PDF
ISSN	1744683X
Volume Number	9
Issue Number	9
Journal	Soft Matter
DOI	10.1039/c2sm27143e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Tissue engineering Cytotoxicity Drug delivery Fourier-transform infrared spectroscopy Hydrophobe Soto Self-assembly Amphiphile Amyloid Surface tension Beta sheet Hydrophile Molecular self-assembly Peptide
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics

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