Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles

Siddhartha Shrivastava; Joseph H. Nuffer; Richard W. Siegel; Jonathan S. Dordick

doi:10.1021/nl2044524

Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles

Siddhartha Shrivastava
, Joseph H. Nuffer
, Richard W. Siegel
, Jonathan S. Dordick

Research output: Contribution to journal › Article › peer-review

57 Scopus citations

Abstract

Figure Persented: We describe a method for determining the orientation of cytochrome c, RNase A, and lysozyme on silica nanoparticles (SNPs) using chemical modification combined with proteolysis-mass spectrometry. The proteins interacted with SNPs through preferential adsorption sites, which are dependent on SNP diameter; 4 nm SNPs induce greater structural stabilization than 15 nm particles, presumably due to greater surface curvature of the former. These results suggest that nanoparticle size and protein structure influence protein orientation on SNPs.

Original language	English
Pages (from-to)	1583-1587
Number of pages	5
Journal	Nano Letters
Volume	12
Issue number	3
DOIs	https://doi.org/10.1021/nl2044524
State	Published - 14 Mar 2012
Externally published	Yes

Keywords

Silica nanoparticles
chemical modification
protein orientation
quantitative proteomics

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10.1021/nl2044524

Cite this

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title = "Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles",

abstract = "Figure Persented: We describe a method for determining the orientation of cytochrome c, RNase A, and lysozyme on silica nanoparticles (SNPs) using chemical modification combined with proteolysis-mass spectrometry. The proteins interacted with SNPs through preferential adsorption sites, which are dependent on SNP diameter; 4 nm SNPs induce greater structural stabilization than 15 nm particles, presumably due to greater surface curvature of the former. These results suggest that nanoparticle size and protein structure influence protein orientation on SNPs.",

keywords = "Silica nanoparticles, chemical modification, protein orientation, quantitative proteomics",

author = "Siddhartha Shrivastava and Nuffer, \{Joseph H.\} and Siegel, \{Richard W.\} and Dordick, \{Jonathan S.\}",

year = "2012",

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doi = "10.1021/nl2044524",

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volume = "12",

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journal = "Nano Letters",

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T1 - Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles

AU - Shrivastava, Siddhartha

AU - Nuffer, Joseph H.

AU - Siegel, Richard W.

AU - Dordick, Jonathan S.

PY - 2012/3/14

Y1 - 2012/3/14

N2 - Figure Persented: We describe a method for determining the orientation of cytochrome c, RNase A, and lysozyme on silica nanoparticles (SNPs) using chemical modification combined with proteolysis-mass spectrometry. The proteins interacted with SNPs through preferential adsorption sites, which are dependent on SNP diameter; 4 nm SNPs induce greater structural stabilization than 15 nm particles, presumably due to greater surface curvature of the former. These results suggest that nanoparticle size and protein structure influence protein orientation on SNPs.

AB - Figure Persented: We describe a method for determining the orientation of cytochrome c, RNase A, and lysozyme on silica nanoparticles (SNPs) using chemical modification combined with proteolysis-mass spectrometry. The proteins interacted with SNPs through preferential adsorption sites, which are dependent on SNP diameter; 4 nm SNPs induce greater structural stabilization than 15 nm particles, presumably due to greater surface curvature of the former. These results suggest that nanoparticle size and protein structure influence protein orientation on SNPs.

KW - Silica nanoparticles

KW - chemical modification

KW - protein orientation

KW - quantitative proteomics

UR - https://www.scopus.com/pages/publications/84858240349

U2 - 10.1021/nl2044524

DO - 10.1021/nl2044524

M3 - Article

C2 - 22296027

AN - SCOPUS:84858240349

SN - 1530-6984

VL - 12

SP - 1583

EP - 1587

JO - Nano Letters

JF - Nano Letters

IS - 3

ER -

Position-specific chemical modification and quantitative proteomics disclose protein orientation adsorbed on silica nanoparticles

Abstract

Keywords

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