Molecular modeling and experimental approaches toward designing a minimalist protein having Fc-binding activity of Staphylococcal protein A
Protein A (PA), a cell wall constituent of Staphylococcus aureus, has got the unique property of binding with the Fc fragment of IgG from various species. The sequence data indicate five highly homologous Fc-binding regions in protein A. Computer sequence analysis provided the tryptic and chymotrypt...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1999-03, Vol.256 (1), p.6-12 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Sengupta, J Sinha, P Mukhopadhyay, C Ray, P K |
| description | Protein A (PA), a cell wall constituent of Staphylococcus aureus, has got the unique property of binding with the Fc fragment of IgG from various species. The sequence data indicate five highly homologous Fc-binding regions in protein A. Computer sequence analysis provided the tryptic and chymotryptic fragments of IgG-binding domains of protein A. Molecular modeling in conjunction with molecular mechanical calculation has been used to search for the smallest possible proteolytic fragments of PA, still retaining Fc-binding activity. A 20-residue peptide (typtic fragment) and a 16-residue peptide (chymotryptic fragment) have been indicated, by molecular modeling studies, to possess IgG-binding affinity comparable to that of the B domain of Protein A. Binding of a 20-residue peptide has been substantiated experimentally by immunoprecipitation, capillary electrophoresis, and circular dichroism spectroscopic analyses. |
| doi_str_mv | 10.1006/bbrc.1999.0198 |
| format | Article |
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The sequence data indicate five highly homologous Fc-binding regions in protein A. Computer sequence analysis provided the tryptic and chymotryptic fragments of IgG-binding domains of protein A. Molecular modeling in conjunction with molecular mechanical calculation has been used to search for the smallest possible proteolytic fragments of PA, still retaining Fc-binding activity. A 20-residue peptide (typtic fragment) and a 16-residue peptide (chymotryptic fragment) have been indicated, by molecular modeling studies, to possess IgG-binding affinity comparable to that of the B domain of Protein A. Binding of a 20-residue peptide has been substantiated experimentally by immunoprecipitation, capillary electrophoresis, and circular dichroism spectroscopic analyses.</description><identifier>ISSN: 0006-291X</identifier><identifier>DOI: 10.1006/bbrc.1999.0198</identifier><identifier>PMID: 10066414</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Chymotrypsin - metabolism ; Circular Dichroism ; Drug Design ; Electrophoresis, Capillary ; Humans ; Hydrogen Bonding ; Immunoglobulin Fc Fragments - metabolism ; Immunoglobulin G - metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments - chemical synthesis ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Precipitin Tests ; Protein Binding ; Protein Structure, Secondary ; Software ; Staphylococcal Protein A - chemistry ; Staphylococcal Protein A - metabolism ; Staphylococcus aureus ; Thermodynamics ; Trypsin - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1999-03, Vol.256 (1), p.6-12</ispartof><rights>Copyright 1999 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10066414$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sengupta, J</creatorcontrib><creatorcontrib>Sinha, P</creatorcontrib><creatorcontrib>Mukhopadhyay, C</creatorcontrib><creatorcontrib>Ray, P K</creatorcontrib><title>Molecular modeling and experimental approaches toward designing a minimalist protein having Fc-binding activity of Staphylococcal protein A</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Protein A (PA), a cell wall constituent of Staphylococcus aureus, has got the unique property of binding with the Fc fragment of IgG from various species. The sequence data indicate five highly homologous Fc-binding regions in protein A. Computer sequence analysis provided the tryptic and chymotryptic fragments of IgG-binding domains of protein A. Molecular modeling in conjunction with molecular mechanical calculation has been used to search for the smallest possible proteolytic fragments of PA, still retaining Fc-binding activity. A 20-residue peptide (typtic fragment) and a 16-residue peptide (chymotryptic fragment) have been indicated, by molecular modeling studies, to possess IgG-binding affinity comparable to that of the B domain of Protein A. Binding of a 20-residue peptide has been substantiated experimentally by immunoprecipitation, capillary electrophoresis, and circular dichroism spectroscopic analyses.</description><subject>Amino Acid Sequence</subject><subject>Chymotrypsin - metabolism</subject><subject>Circular Dichroism</subject><subject>Drug Design</subject><subject>Electrophoresis, Capillary</subject><subject>Humans</subject><subject>Hydrogen Bonding</subject><subject>Immunoglobulin Fc Fragments - metabolism</subject><subject>Immunoglobulin G - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemical synthesis</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>Software</subject><subject>Staphylococcal Protein A - chemistry</subject><subject>Staphylococcal Protein A - metabolism</subject><subject>Staphylococcus aureus</subject><subject>Thermodynamics</subject><subject>Trypsin - metabolism</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0D1PAzEMBuAMIFoKKyPKxHYlvq9exqqigFTEAEhsJyfna4NyH1zSQn8Df5praWcmS_ZjW3oZuwIxBiHSW6U6PQYp5ViAzE7YUPTdIJTwPmDnzn0IARCn8owNdjyNIR6yn6fGkl5b7HjVFGRNveRYF5y-W-pMRbVHy7Ftuwb1ihz3zRd2BS_ImWW9x7wytanQGud5zzyZmq9ws5vNdaBMXeyZ9mZj_JY3JX_x2K62ttGN1v3149L0gp2WaB1dHuqIvc3vXmcPweL5_nE2XQRtGGU-gCRSkKRxrMtSg86UDCchlIgTLIsIQ4lxREQlCKUylWkCLXsfJYWaSOiHI3bzd7f__Lkm5_PKOE3WYk3N2uWpTEUCAv6FMIFMRCLp4fUBrlVFRd720WG3zY85R7_98YGm</recordid><startdate>19990305</startdate><enddate>19990305</enddate><creator>Sengupta, J</creator><creator>Sinha, P</creator><creator>Mukhopadhyay, C</creator><creator>Ray, P K</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19990305</creationdate><title>Molecular modeling and experimental approaches toward designing a minimalist protein having Fc-binding activity of Staphylococcal protein A</title><author>Sengupta, J ; 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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acid Sequence Chymotrypsin - metabolism Circular Dichroism Drug Design Electrophoresis, Capillary Humans Hydrogen Bonding Immunoglobulin Fc Fragments - metabolism Immunoglobulin G - metabolism Models, Molecular Molecular Sequence Data Peptide Fragments - chemical synthesis Peptide Fragments - chemistry Peptide Fragments - metabolism Precipitin Tests Protein Binding Protein Structure, Secondary Software Staphylococcal Protein A - chemistry Staphylococcal Protein A - metabolism Staphylococcus aureus Thermodynamics Trypsin - metabolism |
| title | Molecular modeling and experimental approaches toward designing a minimalist protein having Fc-binding activity of Staphylococcal protein A |
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