Reversible “Irreversible” Inhibition of Chymotrypsin Using Nanoparticle Receptors
Anionically functionalized amphiphilic nanoparticles efficiently inhibit chymotrypsin through electrostatic binding followed by protein denaturation. We demonstrate the ability to disrupt this “irreversible” inhibition of chymotrypsin through modification of the nanoparticle surface using cationic s...
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| Veröffentlicht in: | Journal of the American Chemical Society 2003-11, Vol.125 (44), p.13387-13391 |
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| container_end_page | 13391 |
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| container_issue | 44 |
| container_start_page | 13387 |
| container_title | Journal of the American Chemical Society |
| container_volume | 125 |
| creator | Fischer, Nicholas O Verma, Ayush Goodman, Catherine M Simard, Joseph M Rotello, Vincent M |
| description | Anionically functionalized amphiphilic nanoparticles efficiently inhibit chymotrypsin through electrostatic binding followed by protein denaturation. We demonstrate the ability to disrupt this “irreversible” inhibition of chymotrypsin through modification of the nanoparticle surface using cationic surfactants. Up to 50% of original chymotrypsin activity is rescued upon long-chain surfactant addition. Dynamic light-scattering studies demonstrate that chymotrypsin is released from the nanoparticle surface. The conformation of the rescued chymotrypsin was characterized by fluorescence and fluorescence anisotropy, indicating that chymotrypsin regains a high degree of native structure upon surfactant addition. |
| doi_str_mv | 10.1021/ja0352505 |
| format | Article |
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We demonstrate the ability to disrupt this “irreversible” inhibition of chymotrypsin through modification of the nanoparticle surface using cationic surfactants. Up to 50% of original chymotrypsin activity is rescued upon long-chain surfactant addition. Dynamic light-scattering studies demonstrate that chymotrypsin is released from the nanoparticle surface. 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Am. Chem. Soc</addtitle><description>Anionically functionalized amphiphilic nanoparticles efficiently inhibit chymotrypsin through electrostatic binding followed by protein denaturation. We demonstrate the ability to disrupt this “irreversible” inhibition of chymotrypsin through modification of the nanoparticle surface using cationic surfactants. Up to 50% of original chymotrypsin activity is rescued upon long-chain surfactant addition. Dynamic light-scattering studies demonstrate that chymotrypsin is released from the nanoparticle surface. The conformation of the rescued chymotrypsin was characterized by fluorescence and fluorescence anisotropy, indicating that chymotrypsin regains a high degree of native structure upon surfactant addition.</description><subject>Biological and medical sciences</subject><subject>Carboxylic Acids - chemistry</subject><subject>Chymotrypsin - antagonists & inhibitors</subject><subject>Fluorescence Polarization</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gold - chemistry</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Molecular biophysics</subject><subject>Nanotechnology</subject><subject>Particle Size</subject><subject>Protein Denaturation</subject><subject>Static Electricity</subject><subject>Surface Properties</subject><subject>Surface-Active Agents - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkLtOwzAUhi0EouUy8AIoC0gMAV9iJx1RuVWqAEFZulhOegwuaRzsFNGtDwIv1yfBqFW7sJyjY3_69OtH6Ijgc4IpuRgrzDjlmG-hNuEUx5xQsY3aGGMap5lgLbTn_TicCc3ILmqRhGcMs6SNXp7gE5w3eQnRYv7dc259L-Y_Ua96M7lpjK0iq6Pu22xiGzervamilzBeo3tV2Vq5xhRB8AQF1I11_gDtaFV6OFztfTS4uR507-L-w22ve9mPVUJEE2sOuiA4E4QRnIdQPNc8C68UpyPKs5zzEFhAqkAnHQYJ5B2u-UgInWnosH10utTWzn5MwTdyYnwBZakqsFMvU8IoYQkN4NkSLJz13oGWtTMT5WaSYPlXoVxXGNjjlXSaT2C0IVedBeBkBShfqFI7VRXGbzhOBUnYnyhecsY38LX-V-5dipSlXA4en2Wf4OEVG6ZSbLyq8HJsp64K1f0T8Bfk3JVv</recordid><startdate>20031105</startdate><enddate>20031105</enddate><creator>Fischer, Nicholas O</creator><creator>Verma, Ayush</creator><creator>Goodman, Catherine M</creator><creator>Simard, Joseph M</creator><creator>Rotello, Vincent M</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20031105</creationdate><title>Reversible “Irreversible” Inhibition of Chymotrypsin Using Nanoparticle Receptors</title><author>Fischer, Nicholas O ; Verma, Ayush ; Goodman, Catherine M ; Simard, Joseph M ; Rotello, Vincent M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a416t-f5efc10861310b1455bf58f5e207d258b554286e7aef493e4eb95f5d66f8fe93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Biological and medical sciences</topic><topic>Carboxylic Acids - chemistry</topic><topic>Chymotrypsin - antagonists & inhibitors</topic><topic>Fluorescence Polarization</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gold - chemistry</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Molecular biophysics</topic><topic>Nanotechnology</topic><topic>Particle Size</topic><topic>Protein Denaturation</topic><topic>Static Electricity</topic><topic>Surface Properties</topic><topic>Surface-Active Agents - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fischer, Nicholas O</creatorcontrib><creatorcontrib>Verma, Ayush</creatorcontrib><creatorcontrib>Goodman, Catherine M</creatorcontrib><creatorcontrib>Simard, Joseph M</creatorcontrib><creatorcontrib>Rotello, Vincent M</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fischer, Nicholas O</au><au>Verma, Ayush</au><au>Goodman, Catherine M</au><au>Simard, Joseph M</au><au>Rotello, Vincent M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reversible “Irreversible” Inhibition of Chymotrypsin Using Nanoparticle Receptors</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2003-11-05</date><risdate>2003</risdate><volume>125</volume><issue>44</issue><spage>13387</spage><epage>13391</epage><pages>13387-13391</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>Anionically functionalized amphiphilic nanoparticles efficiently inhibit chymotrypsin through electrostatic binding followed by protein denaturation. We demonstrate the ability to disrupt this “irreversible” inhibition of chymotrypsin through modification of the nanoparticle surface using cationic surfactants. Up to 50% of original chymotrypsin activity is rescued upon long-chain surfactant addition. Dynamic light-scattering studies demonstrate that chymotrypsin is released from the nanoparticle surface. 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| source | MEDLINE; American Chemical Society Journals |
| subjects | Biological and medical sciences Carboxylic Acids - chemistry Chymotrypsin - antagonists & inhibitors Fluorescence Polarization Fundamental and applied biological sciences. Psychology Gold - chemistry Interactions. Associations Intermolecular phenomena Molecular biophysics Nanotechnology Particle Size Protein Denaturation Static Electricity Surface Properties Surface-Active Agents - chemistry |
| title | Reversible “Irreversible” Inhibition of Chymotrypsin Using Nanoparticle Receptors |
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