Short polyethylene glycol chains densely bound to soft nanotube channels for inhibition of protein aggregation. Issue 43 (13th April 2016)

• Record Type: Journal Article
• Authors: Kameta, N.; Matsuzawa, T.; Yaoi, K.; Masuda, M.
• Is Part Of: RSC advances. Volume 6:Issue 43(2016)
• Page Start: 36744
• Page End: 36750
• Publication Date: 2016-04-13
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c6ra06793j
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Specific thermal dehydration/rehydration of short polyethylene glycol (PEG) chains densely bound to nanotube channels was useful for aggregation suppression and refolding acceleration of proteins. Abstract : Two-step self-assembly of two different lipids and a short polyethylene glycol (PEG) unit selectively produced molecular monolayer nanotubes with 7–9 nm-diameter nanochannels densely functionalized with short PEG chains. Fluorescence spectroscopy and microscopy using an environmentally responsive probe suggested that the PEG chains in the nanochannel were dehydrated when the temperature was raised above 45–50 °C and rehydrated by cooling to 25 °C, whereas the PEG chains in the bulk solution showed no such dehydration/rehydration behavior in response to variations of temperature. Nanotube channels that became hydrophobic as a result of the dehydration of the interior PEG chains effectively suppressed aggregation of a thermally denatured protein under high temperature conditions. Regeneration of the hydrophilic nanochannels by rehydration of the interior PEG chains allowed the encapsulated protein to be quickly released to the bulk solution and simultaneously facilitated the refolding of the protein.