TY - JOUR
T1 - Harnessing Peptide Binding to Capture and Reclaim Phosphate
AU - Fowler, Whitney C.
AU - Deng, Chuting
AU - Griffen, Gabriella M.
AU - Teodoro, Tess
AU - Guo, Ashley Z.
AU - Zaiden, Michal
AU - Gottlieb, Moshe
AU - De Pablo, Juan J.
AU - Tirrell, Matthew V.
N1 - Publisher Copyright:
©
PY - 2021/3/24
Y1 - 2021/3/24
N2 - With rising consumer demands, society is tapping into wastewater as an innovative source to recycle depleting resources. Novel reclamation technologies have been recently explored for this purpose, including several that optimize natural biological processes for targeted reclamation. However, this emerging field has a noticeable dearth of synthetic material technologies that are programmed to capture, release, and recycle specified targets; and of the novel materials that do exist, synthetic platforms incorporating biologically inspired mechanisms are rare. We present here a prototype of a materials platform utilizing peptide amphiphiles that has been molecularly engineered to sequester, release, and reclaim phosphate through a stimuli-responsive pH trigger, exploiting a protein-inspired binding mechanism that is incorporated directly into the self-assembled material network. This material is able to harvest and controllably release phosphate for multiple cycles of reuse, and it is selective over nitrate and nitrite. We have determined by simulations that the binding conformation of the peptide becomes constrained in the dense micelle corona at high pH such that phosphate is expelled when it otherwise would be preferentially bound. However, at neutral pH, this dense structure conversely employs multichain binding to further stabilize phosphate when it would otherwise be unbound, opening opportunities for higher-order conformational binding design to be engineered into this controllably packed corona. With this work, we are pioneering a new platform to be readily altered to capture other valuable targets, presenting a new class of capture and release materials for recycling resources on the nanoscale.
AB - With rising consumer demands, society is tapping into wastewater as an innovative source to recycle depleting resources. Novel reclamation technologies have been recently explored for this purpose, including several that optimize natural biological processes for targeted reclamation. However, this emerging field has a noticeable dearth of synthetic material technologies that are programmed to capture, release, and recycle specified targets; and of the novel materials that do exist, synthetic platforms incorporating biologically inspired mechanisms are rare. We present here a prototype of a materials platform utilizing peptide amphiphiles that has been molecularly engineered to sequester, release, and reclaim phosphate through a stimuli-responsive pH trigger, exploiting a protein-inspired binding mechanism that is incorporated directly into the self-assembled material network. This material is able to harvest and controllably release phosphate for multiple cycles of reuse, and it is selective over nitrate and nitrite. We have determined by simulations that the binding conformation of the peptide becomes constrained in the dense micelle corona at high pH such that phosphate is expelled when it otherwise would be preferentially bound. However, at neutral pH, this dense structure conversely employs multichain binding to further stabilize phosphate when it would otherwise be unbound, opening opportunities for higher-order conformational binding design to be engineered into this controllably packed corona. With this work, we are pioneering a new platform to be readily altered to capture other valuable targets, presenting a new class of capture and release materials for recycling resources on the nanoscale.
UR - http://www.scopus.com/inward/record.url?scp=85103474391&partnerID=8YFLogxK
U2 - 10.1021/jacs.1c01241
DO - 10.1021/jacs.1c01241
M3 - Article
C2 - 33721492
AN - SCOPUS:85103474391
SN - 0002-7863
VL - 143
SP - 4440
EP - 4450
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 11
ER -