2009
DOI: 10.1039/b815775h
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Structural characterization of α-lactalbumin nanotubes

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Cited by 36 publications
(21 citation statements)
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“…PNTs derived from α ‐lactalbumin appear to be 10‐start helical right‐handed structures with outer and inner diameters of 20 and 8.7 nm, respectively. Mass spectral analysis indicated that PNT subunits were composed of a mixture of products from proteolysis of the α ‐lactalbumin precursor 68. While this result may affect PNT homogeneity, it does demonstrate the potential for proteolytic triggering of PNT generation from a precursor protein, for example, a fusion protein.…”
Section: Other Protein Nanotubesmentioning
confidence: 98%
See 1 more Smart Citation
“…PNTs derived from α ‐lactalbumin appear to be 10‐start helical right‐handed structures with outer and inner diameters of 20 and 8.7 nm, respectively. Mass spectral analysis indicated that PNT subunits were composed of a mixture of products from proteolysis of the α ‐lactalbumin precursor 68. While this result may affect PNT homogeneity, it does demonstrate the potential for proteolytic triggering of PNT generation from a precursor protein, for example, a fusion protein.…”
Section: Other Protein Nanotubesmentioning
confidence: 98%
“…TRAP monomers form 11‐mer rings that polymerize into PNTs of approximately 8 nm in diameter 67. A third example of a non‐pilin PNT is the observed self‐assembly of the milk protein α ‐lactalbumin,68 where a partial proteolytic hydrolysis acts as a trigger for self‐assembly. PNTs derived from α ‐lactalbumin appear to be 10‐start helical right‐handed structures with outer and inner diameters of 20 and 8.7 nm, respectively.…”
Section: Other Protein Nanotubesmentioning
confidence: 99%
“…Globular proteins in food may lose their native states during the extraction, isolation, and purification of functional food ingredients (such as milk, egg, or soy protein concentrates or isolates) or after incorporation into a food product due to changes in their environment, such as pH, ionic strength, solvent type, temperature, adsorption to interfaces, high pressure, dehydration, or chemical treatments (Damodaran 1996). Understanding the specific factors and mechanisms of protein aggregation is helpful in the rational formation of protein structures, such as spheroids, filaments (Akkermans and others 2007; Jung and others 2008), and nano‐tubes (Graveland‐Bikker and others 2009).…”
Section: Structural Design Principlesmentioning
confidence: 99%
“…On the other hand, thin filaments (dia about 1 to 10 nm) (Arnaudov and others 2003; Gosal and others 2004; Akkermans and others 2008) tend to be formed under conditions where there is a relatively strong electrostatic repulsion between the protein molecules: pH ≠ pI and low ionic strength (Belloque and Smith 1998; Verheul and Roefs 1998; Hoffmann and van Mill 1999; Verheul and others 1999; Foegeding 2006; Donald 2008; Osaka and others 2008). Recently, it has been shown that nano‐tubes can be formed by inducing thermal denaturation and aggregation of enzymatically modified globular proteins (Graveland‐Bikker and others 2009).…”
Section: Structural Design Principlesmentioning
confidence: 99%
“…These are the only food protein nanotubes and are formed in the presence of calcium at neutral pH (Kaya-Celiker and Mallikarjunan 2012). Graveland-Bikker et al (2009) propose the existence of dimeric building blocks which are able to self-assemble into a 10-start, right-handed helix via β-sheet stacking to form the nanotubes. The kind of self-assembly depends strongly on the protein concentration.…”
Section: α-Lactalbumin (α-La)mentioning
confidence: 99%