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Boris L. T. Lau

Researcher at University of Massachusetts Amherst

Publications -  39
Citations -  1617

Boris L. T. Lau is an academic researcher from University of Massachusetts Amherst. The author has contributed to research in topics: Silver nanoparticle & Adsorption. The author has an hindex of 18, co-authored 39 publications receiving 1359 citations. Previous affiliations of Boris L. T. Lau include Duke University & Northwestern University.

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When nanoparticles meet biofilms—interactions guiding the environmental fate and accumulation of nanoparticles

TL;DR: This mini review of NP–biofilm interactions within the aquatic environment highlights key physical, chemical, and biological processes that affect interactions and accumulation of NPs by bacterial biofilms and posit that these biofilm processes present the likely possibility for unique biological and chemical transformations of N Ps.
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Silver nanoparticle-alginate composite beads for point-of-use drinking water disinfection

TL;DR: From the results of this study, it was identified that SGR may be the best choice among all three different synthesis approaches in that the SGR beads can achieve satisfactory bactericidal performance with a relatively low material consumption rate.
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Effects of Humic Substances on Precipitation and Aggregation of Zinc Sulfide Nanoparticles

TL;DR: Results of this study suggest that the composition and source of NOM are key factors that contribute to the stabilization and persistence of zinc sulfide nanoparticles in the aquatic environment.
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Relative Importance of the Humic and Fulvic Fractions of Natural Organic Matter in the Aggregation and Deposition of Silver Nanoparticles

TL;DR: To understand the relative impact of humic (HA) and fulvic fraction of NOM on the stability and mobility of silver nanoparticles (AgNPs), a combination of dynamic light scattering and quartz crystal microgravimetry with dissipation monitoring was used.
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Effects of surface compositional and structural heterogeneity on nanoparticle-protein interactions: different protein configurations.

TL;DR: The results of this study point to the potential for utilizing nanoscale manipulation of NP surfaces to control the resulting NP-protein interactions.