Aquamelt

An aquamelt is a naturally hydrated polymeric material that is able to solidify at environmental temperatures through a controlled stress input (be it mechanical or chemical).

They are unique in being able to “lock in” work applied to them through an alteration in hydrogen bonding, which enables them to be processed with approximately 1000 times less energy than standard polymers.[1] This has been recently shown for an archetypal biopolymer, silk,[2] however the mechanism for solidification is thought to be inherent to many other biological materials.[3][4]

Discovery and mechanism

Aquamelts were defined as a new class of polymeric material as a result of a comparison between the spinning feedstock of the Chinese silkworm (Bombyx mori) and molten high-density polyethylene (HDPE)[2] using shear induced polarised light imaging (SIPLI).[5]

The current understanding of shear induced fibrillation requires polymer chains to undergo the following series of steps i) long-chain molecules are stretched, ii) and form persistent point nuclei, which iii) align under flow into rows and then iv) grow to create a crystalline fibrils.[2] For these fibrils to remain, the temperature of the sample must be lowered to below the polymers melt point. This process is analogous to the fibrilogenesis of natural silk-polymers in which proteins align (refold), nucleate (denature), and crystallize (aggregate). However, for silks, fibrils persist without the need for a drop in temperature.[6][7]

From a macromolecular perspective the two processes are thought to be similar due to a native protein's unique interaction with its closely bound water.[3][4] Much like an individual polymer chain in a melt, a native protein and its closely bound water molecules may be considered not as a solution but as a single processable entity, a nanocomposite termed an "aquamelt".

The differences between a typical polymer and an aquamelt are highlighted by an aquamelt's ability to solidify in response to stress at environmental temperatures. This occurs when the stress applied is sufficient to separate the closely bound water from the protein, splitting the nanocomposite. This results in conformational changes to the protein and an increased probability to form hydrogen bonding between protein chains and subsequent solidification.[4] Multiscale structures, i.e., fibrils or foams are the result of a combination of directional stress fields and the self-assembly properties of the aquamelt.[7][8]

Potential uses

Aquamelts offer several advantages over current solutions to synthetic polymer production. Firstly they are naturally sourced, with no reliance on oil for production and are recyclable and biodegradable. Secondly they can be processed at room temperatures and pressures resulting in only water as a by-product from the solidification process. Thirdly work calculations performed on silk and high-density polyethylene feedstocks revealed a tenfold difference in the amount of shear energy required in order to initiate solidification.[9] When processing temperature is taken into account the difference in energy requirements to undergo solidification is a thousandfold less for aquamelts than synthetic polymers.[1]

gollark: ++remind 22h adjust (actual, real)
gollark: ++remind 11h adjust or else.
gollark: Okay.
gollark: Anything else I can put at the bottom of the iceberg?
gollark: It's highly subjective and I wanted to balance things between layers.

References
  1. "How Silkworms Beat Polymer Scientists - The Aquamelt Secret". Science Debate. 25 November 2011. Retrieved 10 April 2012.
  2. Holland, C; Vollrath, F; Ryan, A; Mykhaylyk, O (2012). "Silk and Synthetic Polymers: Reconciling 100 Degrees of Separation". Advanced Materials. 24 (1): 105–109. doi:10.1002/adma.201103664. PMID 22109705.
  3. Porter, D; Vollrath, F (2008). "The role of kinetics of water and amide bonding in protein stability". Soft Matter. 4 (1): 328–336. Bibcode:2008SMat....4..328P. doi:10.1039/B713972A.
  4. Porter, D; Vollrath, F (2012). "Water mobility, denaturation and the glass transition in proteins". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824 (6): 785–791. doi:10.1016/j.bbapap.2012.03.007. PMID 22465032.
  5. Mykhaylyk, O (2010). "Time-resolved polarized light imaging of sheared materials: application to polymer crystallization". Soft Matter. 6 (18): 4430–4440. Bibcode:2010SMat....6.4430M. doi:10.1039/C0SM00332H.
  6. Boulet-Audet, M; Vollrath, F; Holland, C (2011). "Rheo-attenuated total reflectance infrared spectroscopy: a new tool to study biopolymers". Physical Chemistry Chemical Physics. 13 (9): 3979–3984. Bibcode:2011PCCP...13.3979B. doi:10.1039/C0CP02599B. PMID 21240437.
  7. Holland, C; Urbach, J; Blair, D (2012). "Direct Visualization of Shear Dependent Silk Fibrillogenesis" (PDF). Soft Matter. 8 (9): 2590–2594. Bibcode:2012SMat....8.2590H. doi:10.1039/C2SM06886A.
  8. Guan, J; Porter, D; K, Tian; Zhengzhong, S; Chen, X (2010). "Morphology and mechanical properties of soy protein scaffolds made by directional freezing". Journal of Applied Polymer Science. 118 (3): 328–336. doi:10.1002/app.32579.
  9. Chelsea Whyte (23 November 2011). "Face-to-face with the super-efficient silkworm". New Scientist. Retrieved 10 April 2012.
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