Aggregation of silica nanoparticles directed by adsorption of lysozyme

The interaction of the globular protein lysozyme with silica nanoparticles of diameter 20 nm was studied in a pH range between the isoelectric points (IEPs) of silica and the protein (pH 3-11). The adsorption affinity and capacity of lysozyme on the silica particles is increasing progressively with...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 27(2011), 16 vom: 16. Aug., Seite 9823-33
1. Verfasser: Bharti, Bhuvnesh (VerfasserIn)
Weitere Verfasser: Meissner, Jens, Findenegg, Gerhard H
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Silicon Dioxide 7631-86-9 Muramidase EC 3.2.1.17
LEADER 01000naa a22002652 4500
001 NLM209693207
003 DE-627
005 20231224010258.0
007 cr uuu---uuuuu
008 231224s2011 xx |||||o 00| ||eng c
024 7 |a 10.1021/la201898v  |2 doi 
028 5 2 |a pubmed24n0699.xml 
035 |a (DE-627)NLM209693207 
035 |a (NLM)21728288 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Bharti, Bhuvnesh  |e verfasserin  |4 aut 
245 1 0 |a Aggregation of silica nanoparticles directed by adsorption of lysozyme 
264 1 |c 2011 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 09.01.2012 
500 |a Date Revised 09.08.2011 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a The interaction of the globular protein lysozyme with silica nanoparticles of diameter 20 nm was studied in a pH range between the isoelectric points (IEPs) of silica and the protein (pH 3-11). The adsorption affinity and capacity of lysozyme on the silica particles is increasing progressively with pH, and the adsorbed protein induces bridging aggregation of the silica particles. Structural properties of the aggregates were studied as a function of pH at a fixed protein-to-silica concentration ratio which corresponds to a surface concentration of protein well below a complete monolayer in the complete-binding regime at pH > 6. Sedimentation studies indicate the presence of compact aggregates at pH 4-6 and a loose flocculated network at pH 7-9, followed by a sharp decrease of aggregate size near the IEP of lysozyme. The structure of the bridged silica aggregates was studied by cryo-transmission electron microscopy (cryo-TEM) and small-angle X-ray scattering. The structure factor S(q) derived from the scattering profiles displays characteristic features of particles interacting by a short-range attractive potential and can be represented by the square-well Percus-Yevick potential model, with a potential depth not exceeding 3k(B)T 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Silicon Dioxide  |2 NLM 
650 7 |a 7631-86-9  |2 NLM 
650 7 |a Muramidase  |2 NLM 
650 7 |a EC 3.2.1.17  |2 NLM 
700 1 |a Meissner, Jens  |e verfasserin  |4 aut 
700 1 |a Findenegg, Gerhard H  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Langmuir : the ACS journal of surfaces and colloids  |d 1992  |g 27(2011), 16 vom: 16. Aug., Seite 9823-33  |w (DE-627)NLM098181009  |x 1520-5827  |7 nnns 
773 1 8 |g volume:27  |g year:2011  |g number:16  |g day:16  |g month:08  |g pages:9823-33 
856 4 0 |u http://dx.doi.org/10.1021/la201898v  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_22 
912 |a GBV_ILN_350 
912 |a GBV_ILN_721 
951 |a AR 
952 |d 27  |j 2011  |e 16  |b 16  |c 08  |h 9823-33