2020
DOI: 10.1039/d0ra06637k
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Exploring the effect of a peptide additive on struvite formation and morphology: a high-throughput method

Abstract: A high-throughput platform was developed to analyze struvite formation, finding that peptide addition modulates growth in a potentially favorable way.

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Cited by 4 publications
(17 citation statements)
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“…The shADP5 peptide was shown previously to increase the formation constant and yield parameter of struvite, but binding to struvite crystals was not explored. 19 Here, we modified the peptide by capping it with a cysteine residue, C-shADP5. This peptide was then immobilized onto Au mesh and chosen due to its reliable thiol binding mechanism.…”
Section: ■ Results and Discussionmentioning
confidence: 99%
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“…The shADP5 peptide was shown previously to increase the formation constant and yield parameter of struvite, but binding to struvite crystals was not explored. 19 Here, we modified the peptide by capping it with a cysteine residue, C-shADP5. This peptide was then immobilized onto Au mesh and chosen due to its reliable thiol binding mechanism.…”
Section: ■ Results and Discussionmentioning
confidence: 99%
“…Peptides were designed based on our previous study. 19 To facilitate Au binding, a cysteine residue was placed on the N-terminus of the peptide followed by three glycine residues as spacers. The final sequence of the peptide is: CGGGSYENSH-QAINVDRT and its primary structure shown in Figure S1.…”
Section: ■ Experimental Materials and Methodsmentioning
confidence: 99%
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