2017
DOI: 10.1016/j.jcis.2017.07.046
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Impact of carbon quantum dots on dynamic properties of BSA and BSA/DPPC adsorption layers

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Cited by 12 publications
(6 citation statements)
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“…The occupation of the (NH 4 ) 2 SO 4 , NH 4 HSO 4 , and H 2 O species at the active sites of the catalysts led to inactivation of the catalyst. On the other hand, the capability of N-CQDs and Pal acting as adsorbents for SO 2 and H 2 O may prevent NH 3 from being sulfated, so as to avoid the accumulation of (NH 4 ) 2 SO 4 or NH 4 HSO 4 . After stopping SO 2 and H 2 O, both catalysts demonstrate significant recovery of NO x conversion. This indicates that the inhibition is reversible with competitive adsorption of SO 2 and NO x molecules on the catalysts because of their similar adsorption characteristics …”
Section: Resultsmentioning
confidence: 99%
“…The occupation of the (NH 4 ) 2 SO 4 , NH 4 HSO 4 , and H 2 O species at the active sites of the catalysts led to inactivation of the catalyst. On the other hand, the capability of N-CQDs and Pal acting as adsorbents for SO 2 and H 2 O may prevent NH 3 from being sulfated, so as to avoid the accumulation of (NH 4 ) 2 SO 4 or NH 4 HSO 4 . After stopping SO 2 and H 2 O, both catalysts demonstrate significant recovery of NO x conversion. This indicates that the inhibition is reversible with competitive adsorption of SO 2 and NO x molecules on the catalysts because of their similar adsorption characteristics …”
Section: Resultsmentioning
confidence: 99%
“…At a higher concentration (12 nM) of hydrophilic (MUA) GNPs, the VSFG intensity of interfacial water molecules further decreases and approaches zero. This results in a change in the orientation of interfacial water molecules and/or removal of water from the interface. , Lai et al also reported a similar phenomenon, where high concentrations of hydrophilic NPs led to an increase in serum protein adsorption at the interface, resulting in changes in the interfacial properties of the protein . Additionally, the increase in surface pressure of the DPPG monolayer observed by adding hydrophilic (MUA) GNPs (Figure S6a) indicates accumulation of HSA at the interface at higher concentration (12 nM) of GNPs.…”
Section: Resultsmentioning
confidence: 89%
“…82,83 Lai et al also reported a similar phenomenon, where high concentrations of hydrophilic NPs led to an increase in serum protein adsorption at the interface, resulting in changes in the interfacial properties of the protein. 84 Additionally, the increase in surface pressure of the DPPG monolayer observed by adding hydrophilic (MUA) GNPs (Figure S6a) indicates accumulation of HSA at the interface at higher concentration (12 nM) of GNPs. Similar results are observed for hydro-phobic (UDT) GNPs at pH 3 as shown in Figure 5b, indicating that hydrophobic GNPs also lead to the adsorption of the HSA at the lipid interface leading to a reduction in the SFG intensity of water molecule due to the hydrophobic interaction between the alkyl chain of the DPPG monolayer and the HSA protein with the hydrophobic chain of the hydrophobic (UDT) GNPs.…”
Section: ■ Introductionmentioning
confidence: 98%
“…The BSA molecule consists of three homologous domains (I, II, and III), which are divided into nine rings (L1‐L9) by 17 disulfide bonds [33] . BSA contains tryptophan 134 and 212, which are inherently fluorescent and embedded in the subdomain IIA and first subdomain IB, respectively [34] . BSA is used as an HSA replacing model for biochemistry, biophysical chemistry, and physical chemistry studies due to its high structural resemblance.…”
Section: Introductionmentioning
confidence: 99%