2009
DOI: 10.1021/la804175h
|View full text |Cite
|
Sign up to set email alerts
|

Peptide Nanotube Nematic Phase

Abstract: The self-assembly of the trifluoroacetate salt of the short peptide (ala)6-lys (A6K) in water has been investigated by cryo-transmission electron microscopy and small-angle X-ray scattering. For concentrations below ca. 12%, the peptide does not self-assemble but forms a molecularly dispersed solution. Above this critical concentration, however, A6K self-assembles into several-micrometer-long hollow nanotubes with a monodisperse cross-sectional radius of 26 nm. Because the peptides carry a positive charge, the… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

3
77
0
3

Year Published

2010
2010
2016
2016

Publication Types

Select...
10

Relationship

0
10

Authors

Journals

citations
Cited by 78 publications
(83 citation statements)
references
References 20 publications
(26 reference statements)
3
77
0
3
Order By: Relevance
“…The latter is predominantly occupied by charged and polar amino acids; these are: arginine (R), [6,7] histidine (H), [7,8] lysine (K), [9][10][11][12][13][14][15] aspartic acid (D), [16,17] glutamic acid (E), [11,18] serine (S), threonine (T), asparagine (N), glutamine (Q), and cysteine (C). [13] The design of the hydrophobic part is based on amino acids with neutral and nonpolar side-chains such as glycine (G), [16] alanine (A), [15,19] valine (V), [17,20] leucine (L), [9,17] isoleucine (I), [21] methionine (M), phenylalanine (F), [22,23] tyrosine (Y), and tryptophan (W). [7,[10][11][12][13][14]23] Depending on the hydrophobic to hydrophilic ratio and the sequence, various self-assembled structures can be constructed -as indicated in the associated references for the above amino acids -although the hydrophobicity is moderated by the polar character of the peptide's backbone.…”
Section: Introductionmentioning
confidence: 99%
“…The latter is predominantly occupied by charged and polar amino acids; these are: arginine (R), [6,7] histidine (H), [7,8] lysine (K), [9][10][11][12][13][14][15] aspartic acid (D), [16,17] glutamic acid (E), [11,18] serine (S), threonine (T), asparagine (N), glutamine (Q), and cysteine (C). [13] The design of the hydrophobic part is based on amino acids with neutral and nonpolar side-chains such as glycine (G), [16] alanine (A), [15,19] valine (V), [17,20] leucine (L), [9,17] isoleucine (I), [21] methionine (M), phenylalanine (F), [22,23] tyrosine (Y), and tryptophan (W). [7,[10][11][12][13][14]23] Depending on the hydrophobic to hydrophilic ratio and the sequence, various self-assembled structures can be constructed -as indicated in the associated references for the above amino acids -although the hydrophobicity is moderated by the polar character of the peptide's backbone.…”
Section: Introductionmentioning
confidence: 99%
“…Other candidate organic crystals that can have titratable surface or near-surface groups include crystals of small dicarboxylic acids that have been probed with AFM, such as the calcium oxalate monohydrate and dihydrate crystals found in kidney stones [76], and cocrystals containing glutarate [77]. Assemblies of small peptides, some of which spontaneously form large cylindrical structures with exposed titratable side chains [78,79], could be another context in which surface protonation patterns like those simulated here may form under appropriate solution conditions. Facets of oxide crystals in water represent another possibility [80,81].…”
Section: Further Discussion and Conclusionmentioning
confidence: 99%
“…The self-assembly of AnK is concentration dependent. A6K was found to self-assemble above a critical concentration in aqueous solutions and form hollow nanotubes with a radius of 26 nm (Figure 2C), followed by a transition to a nematic lamellar phase with increasing peptide concentration (Bucak et al, 2009;Castelletto et al, 2010;Cenker et al, 2011). A4K could not self-assemble to form nanostructures.…”
Section: Small Surfactant-like Peptide Based On the Silk Protein Domainmentioning
confidence: 99%