Streptavidin in Antibody Pretargeting. 3. Comparison of Biotin Binding and Tissue Localization of 1,2-Cyclohexanedione and Succinic Anhydride Modified Recombinant Streptavidin
Recombinant streptavidin (rSAv) is of interest as a carrier of α-emitting radionuclides in pretargeting protocols for cancer therapy. Due to the inherently high kidney localization of rSAv, modification of this protein is required before it can be useful in pretargeting. Previous studies (Wilbur, D....
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Published in: | Bioconjugate chemistry 2002-05, Vol.13 (3), p.611-620 |
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description | Recombinant streptavidin (rSAv) is of interest as a carrier of α-emitting radionuclides in pretargeting protocols for cancer therapy. Due to the inherently high kidney localization of rSAv, modification of this protein is required before it can be useful in pretargeting. Previous studies (Wilbur, D. S., Hamlin, D. K. et al. (1998) Bioconjugate Chem. 9, 322−330) have shown that succinylation of rSAv using succinic anhydride decreases the kidney localization appreciably. In continuing studies, the biotin binding characteristics and biodistribution in mice of rSAv modified by reaction with succinic anhydride (amine modification) or 1,2-cyclohexanedione (arginine modification) have been compared. Modification of rSAv was conducted using 5−50 mol equiv of succinic anhydride and 60−200 mol equiv of 1,2-cyclohexanedione. Most studies were conducted using rSAv modified with the highest quantities of reagents. Succinylation of rSAv did not alter binding with biotin derivatives, but a small increase in the biotin derivative dissociation rate was noted for arginine-modified rSAv. Amino acid analysis of 1,2-cyclohexanedione-treated rSAv indicated about 40% of the arginine residues, or an average of 1.6 residues per subunit, were modified, whereas none of the lysine residues were modified. IEF analyses showed that the pI of the arginine-modified rSAv was 5.3−6, whereas the pI for the succinylated rSAv was approximately 4. Electrospray mass spectral analyses indicated that one to three conjugates of 1,2-cyclohexanedione, and two to three conjugates of succinic anhydride, were obtained per subunit. Both modification reactions resulted in greatly decreasing the kidney localization of rSAv (normally 20−25% ID/g at 4, 24, and 48 h pi). However, the kidney concentration for the succinylated rSAv continued to decrease (5% ID/g to 1.5% ID/g) from 4 to 48 h pi, whereas the concentration (5% ID/g) remained constant over that period of time for the arginine-modified rSAv. In contrast to this, the liver concentration appeared to be slightly higher (3% ID/g vs 2% ID/g) at the later time points for the succinylated rSAv. When less than 50 mol equiv of succinic anhydride were employed in the modification of rSAv, a correlation between increasing kidney localization with decreasing equivalents reacted was observed. Although the differences in the two modified rSAv are not substantial, succinylated rSAv appears to have more favorable properties for pretargeting studies. |
doi_str_mv | 10.1021/bc015574n |
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Comparison of Biotin Binding and Tissue Localization of 1,2-Cyclohexanedione and Succinic Anhydride Modified Recombinant Streptavidin</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)</source><creator>Wilbur, D. Scott ; Hamlin, Donald K ; Meyer, Damon L ; Mallett, Robert W ; Quinn, Janna ; Vessella, Robert L ; Press, Oliver W</creator><creatorcontrib>Wilbur, D. Scott ; Hamlin, Donald K ; Meyer, Damon L ; Mallett, Robert W ; Quinn, Janna ; Vessella, Robert L ; Press, Oliver W</creatorcontrib><description>Recombinant streptavidin (rSAv) is of interest as a carrier of α-emitting radionuclides in pretargeting protocols for cancer therapy. Due to the inherently high kidney localization of rSAv, modification of this protein is required before it can be useful in pretargeting. Previous studies (Wilbur, D. S., Hamlin, D. K. et al. (1998) Bioconjugate Chem. 9, 322−330) have shown that succinylation of rSAv using succinic anhydride decreases the kidney localization appreciably. In continuing studies, the biotin binding characteristics and biodistribution in mice of rSAv modified by reaction with succinic anhydride (amine modification) or 1,2-cyclohexanedione (arginine modification) have been compared. Modification of rSAv was conducted using 5−50 mol equiv of succinic anhydride and 60−200 mol equiv of 1,2-cyclohexanedione. Most studies were conducted using rSAv modified with the highest quantities of reagents. Succinylation of rSAv did not alter binding with biotin derivatives, but a small increase in the biotin derivative dissociation rate was noted for arginine-modified rSAv. Amino acid analysis of 1,2-cyclohexanedione-treated rSAv indicated about 40% of the arginine residues, or an average of 1.6 residues per subunit, were modified, whereas none of the lysine residues were modified. IEF analyses showed that the pI of the arginine-modified rSAv was 5.3−6, whereas the pI for the succinylated rSAv was approximately 4. Electrospray mass spectral analyses indicated that one to three conjugates of 1,2-cyclohexanedione, and two to three conjugates of succinic anhydride, were obtained per subunit. Both modification reactions resulted in greatly decreasing the kidney localization of rSAv (normally 20−25% ID/g at 4, 24, and 48 h pi). However, the kidney concentration for the succinylated rSAv continued to decrease (5% ID/g to 1.5% ID/g) from 4 to 48 h pi, whereas the concentration (5% ID/g) remained constant over that period of time for the arginine-modified rSAv. In contrast to this, the liver concentration appeared to be slightly higher (3% ID/g vs 2% ID/g) at the later time points for the succinylated rSAv. When less than 50 mol equiv of succinic anhydride were employed in the modification of rSAv, a correlation between increasing kidney localization with decreasing equivalents reacted was observed. Although the differences in the two modified rSAv are not substantial, succinylated rSAv appears to have more favorable properties for pretargeting studies.</description><identifier>ISSN: 1043-1802</identifier><identifier>EISSN: 1520-4812</identifier><identifier>DOI: 10.1021/bc015574n</identifier><identifier>PMID: 12009953</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Antibodies, Neoplasm - immunology ; Arginine - chemistry ; Biotin - analogs & derivatives ; Biotin - metabolism ; Biotinylation - methods ; Chromatography, High Pressure Liquid ; Cyclohexanones - chemistry ; Immunoglobulin Fab Fragments - chemistry ; Immunoglobulin Fab Fragments - immunology ; Iodine Radioisotopes - metabolism ; Kidney - metabolism ; Male ; Mass Spectrometry ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Neoplasms, Experimental - immunology ; Recombinant Proteins - metabolism ; Streptavidin - analogs & derivatives ; Streptavidin - metabolism ; Succinates - chemistry ; Tissue Distribution</subject><ispartof>Bioconjugate chemistry, 2002-05, Vol.13 (3), p.611-620</ispartof><rights>Copyright © 2002 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a349t-f7894558beead387ae770588cb930f781d025746db2c8b6c1fab5075fdf7db573</citedby><cites>FETCH-LOGICAL-a349t-f7894558beead387ae770588cb930f781d025746db2c8b6c1fab5075fdf7db573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12009953$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilbur, D. Scott</creatorcontrib><creatorcontrib>Hamlin, Donald K</creatorcontrib><creatorcontrib>Meyer, Damon L</creatorcontrib><creatorcontrib>Mallett, Robert W</creatorcontrib><creatorcontrib>Quinn, Janna</creatorcontrib><creatorcontrib>Vessella, Robert L</creatorcontrib><creatorcontrib>Press, Oliver W</creatorcontrib><title>Streptavidin in Antibody Pretargeting. 3. Comparison of Biotin Binding and Tissue Localization of 1,2-Cyclohexanedione and Succinic Anhydride Modified Recombinant Streptavidin</title><title>Bioconjugate chemistry</title><addtitle>Bioconjugate Chem</addtitle><description>Recombinant streptavidin (rSAv) is of interest as a carrier of α-emitting radionuclides in pretargeting protocols for cancer therapy. Due to the inherently high kidney localization of rSAv, modification of this protein is required before it can be useful in pretargeting. Previous studies (Wilbur, D. S., Hamlin, D. K. et al. (1998) Bioconjugate Chem. 9, 322−330) have shown that succinylation of rSAv using succinic anhydride decreases the kidney localization appreciably. In continuing studies, the biotin binding characteristics and biodistribution in mice of rSAv modified by reaction with succinic anhydride (amine modification) or 1,2-cyclohexanedione (arginine modification) have been compared. Modification of rSAv was conducted using 5−50 mol equiv of succinic anhydride and 60−200 mol equiv of 1,2-cyclohexanedione. Most studies were conducted using rSAv modified with the highest quantities of reagents. Succinylation of rSAv did not alter binding with biotin derivatives, but a small increase in the biotin derivative dissociation rate was noted for arginine-modified rSAv. Amino acid analysis of 1,2-cyclohexanedione-treated rSAv indicated about 40% of the arginine residues, or an average of 1.6 residues per subunit, were modified, whereas none of the lysine residues were modified. IEF analyses showed that the pI of the arginine-modified rSAv was 5.3−6, whereas the pI for the succinylated rSAv was approximately 4. Electrospray mass spectral analyses indicated that one to three conjugates of 1,2-cyclohexanedione, and two to three conjugates of succinic anhydride, were obtained per subunit. Both modification reactions resulted in greatly decreasing the kidney localization of rSAv (normally 20−25% ID/g at 4, 24, and 48 h pi). However, the kidney concentration for the succinylated rSAv continued to decrease (5% ID/g to 1.5% ID/g) from 4 to 48 h pi, whereas the concentration (5% ID/g) remained constant over that period of time for the arginine-modified rSAv. In contrast to this, the liver concentration appeared to be slightly higher (3% ID/g vs 2% ID/g) at the later time points for the succinylated rSAv. When less than 50 mol equiv of succinic anhydride were employed in the modification of rSAv, a correlation between increasing kidney localization with decreasing equivalents reacted was observed. Although the differences in the two modified rSAv are not substantial, succinylated rSAv appears to have more favorable properties for pretargeting studies.</description><subject>Animals</subject><subject>Antibodies, Neoplasm - immunology</subject><subject>Arginine - chemistry</subject><subject>Biotin - analogs & derivatives</subject><subject>Biotin - metabolism</subject><subject>Biotinylation - methods</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cyclohexanones - chemistry</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - immunology</subject><subject>Iodine Radioisotopes - metabolism</subject><subject>Kidney - metabolism</subject><subject>Male</subject><subject>Mass Spectrometry</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Mice, Nude</subject><subject>Neoplasms, Experimental - immunology</subject><subject>Recombinant Proteins - metabolism</subject><subject>Streptavidin - analogs & derivatives</subject><subject>Streptavidin - metabolism</subject><subject>Succinates - chemistry</subject><subject>Tissue Distribution</subject><issn>1043-1802</issn><issn>1520-4812</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNptkc9u1DAQxiMEoqVw4AWQLyAhkcVO4tg5lhVlEYuo2EUcLf-ZbF0Se2s7qMtL8YoYsiockCzNaL6fZ-z5iuIpwQuCK_JaaUwoZY27V5wSWuGy4aS6n3Pc1CXhuDopHsV4jTHuCK8eFiekymlH69Pi5yYF2Cf53RrrUD7nLlnlzQFdBkgy7CBZt1ugeoGWftzLYKN3yPfojfVZycHlizsknUFbG-MEaO21HOwPmexMkldVuTzowV_BrXRgchn-8JtJa-uszjOvDiZYA-ijN7a3YNBn0H5U1kmX0L9PfFw86OUQ4ckxnhVfLt5ul6ty_end--X5upR106WyZ7xrKOUKQJqaMwmMYcq5Vl2Ns0gMrvLCWqMqzVWrSS8VxYz2pmdGUVafFS_mvvvgbyaISYw2ahiG_AM_RcFIy1vatRl8OYM6-BgD9GIf7CjDQRAsfrsj7tzJ7LNj00mNYP6SRzsyUM6AjQlu73QZvomW1YyK7eVGfGV41a4usPiQ-eczL3UU134KLu_kP4N_AbCHqDQ</recordid><startdate>20020501</startdate><enddate>20020501</enddate><creator>Wilbur, D. Scott</creator><creator>Hamlin, Donald K</creator><creator>Meyer, Damon L</creator><creator>Mallett, Robert W</creator><creator>Quinn, Janna</creator><creator>Vessella, Robert L</creator><creator>Press, Oliver W</creator><general>American Chemical Society</general><scope>BSCLL</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>20020501</creationdate><title>Streptavidin in Antibody Pretargeting. 3. Comparison of Biotin Binding and Tissue Localization of 1,2-Cyclohexanedione and Succinic Anhydride Modified Recombinant Streptavidin</title><author>Wilbur, D. Scott ; Hamlin, Donald K ; Meyer, Damon L ; Mallett, Robert W ; Quinn, Janna ; Vessella, Robert L ; Press, Oliver W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a349t-f7894558beead387ae770588cb930f781d025746db2c8b6c1fab5075fdf7db573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Antibodies, Neoplasm - immunology</topic><topic>Arginine - chemistry</topic><topic>Biotin - analogs & derivatives</topic><topic>Biotin - metabolism</topic><topic>Biotinylation - methods</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cyclohexanones - chemistry</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Immunoglobulin Fab Fragments - immunology</topic><topic>Iodine Radioisotopes - metabolism</topic><topic>Kidney - metabolism</topic><topic>Male</topic><topic>Mass Spectrometry</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Mice, Nude</topic><topic>Neoplasms, Experimental - immunology</topic><topic>Recombinant Proteins - metabolism</topic><topic>Streptavidin - analogs & derivatives</topic><topic>Streptavidin - metabolism</topic><topic>Succinates - chemistry</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilbur, D. Scott</creatorcontrib><creatorcontrib>Hamlin, Donald K</creatorcontrib><creatorcontrib>Meyer, Damon L</creatorcontrib><creatorcontrib>Mallett, Robert W</creatorcontrib><creatorcontrib>Quinn, Janna</creatorcontrib><creatorcontrib>Vessella, Robert L</creatorcontrib><creatorcontrib>Press, Oliver W</creatorcontrib><collection>Istex</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>Bioconjugate chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilbur, D. Scott</au><au>Hamlin, Donald K</au><au>Meyer, Damon L</au><au>Mallett, Robert W</au><au>Quinn, Janna</au><au>Vessella, Robert L</au><au>Press, Oliver W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Streptavidin in Antibody Pretargeting. 3. Comparison of Biotin Binding and Tissue Localization of 1,2-Cyclohexanedione and Succinic Anhydride Modified Recombinant Streptavidin</atitle><jtitle>Bioconjugate chemistry</jtitle><addtitle>Bioconjugate Chem</addtitle><date>2002-05-01</date><risdate>2002</risdate><volume>13</volume><issue>3</issue><spage>611</spage><epage>620</epage><pages>611-620</pages><issn>1043-1802</issn><eissn>1520-4812</eissn><abstract>Recombinant streptavidin (rSAv) is of interest as a carrier of α-emitting radionuclides in pretargeting protocols for cancer therapy. Due to the inherently high kidney localization of rSAv, modification of this protein is required before it can be useful in pretargeting. Previous studies (Wilbur, D. S., Hamlin, D. K. et al. (1998) Bioconjugate Chem. 9, 322−330) have shown that succinylation of rSAv using succinic anhydride decreases the kidney localization appreciably. In continuing studies, the biotin binding characteristics and biodistribution in mice of rSAv modified by reaction with succinic anhydride (amine modification) or 1,2-cyclohexanedione (arginine modification) have been compared. Modification of rSAv was conducted using 5−50 mol equiv of succinic anhydride and 60−200 mol equiv of 1,2-cyclohexanedione. Most studies were conducted using rSAv modified with the highest quantities of reagents. Succinylation of rSAv did not alter binding with biotin derivatives, but a small increase in the biotin derivative dissociation rate was noted for arginine-modified rSAv. Amino acid analysis of 1,2-cyclohexanedione-treated rSAv indicated about 40% of the arginine residues, or an average of 1.6 residues per subunit, were modified, whereas none of the lysine residues were modified. IEF analyses showed that the pI of the arginine-modified rSAv was 5.3−6, whereas the pI for the succinylated rSAv was approximately 4. Electrospray mass spectral analyses indicated that one to three conjugates of 1,2-cyclohexanedione, and two to three conjugates of succinic anhydride, were obtained per subunit. Both modification reactions resulted in greatly decreasing the kidney localization of rSAv (normally 20−25% ID/g at 4, 24, and 48 h pi). However, the kidney concentration for the succinylated rSAv continued to decrease (5% ID/g to 1.5% ID/g) from 4 to 48 h pi, whereas the concentration (5% ID/g) remained constant over that period of time for the arginine-modified rSAv. In contrast to this, the liver concentration appeared to be slightly higher (3% ID/g vs 2% ID/g) at the later time points for the succinylated rSAv. When less than 50 mol equiv of succinic anhydride were employed in the modification of rSAv, a correlation between increasing kidney localization with decreasing equivalents reacted was observed. Although the differences in the two modified rSAv are not substantial, succinylated rSAv appears to have more favorable properties for pretargeting studies.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>12009953</pmid><doi>10.1021/bc015574n</doi><tpages>10</tpages></addata></record> |
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subjects | Animals Antibodies, Neoplasm - immunology Arginine - chemistry Biotin - analogs & derivatives Biotin - metabolism Biotinylation - methods Chromatography, High Pressure Liquid Cyclohexanones - chemistry Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - immunology Iodine Radioisotopes - metabolism Kidney - metabolism Male Mass Spectrometry Mice Mice, Inbred BALB C Mice, Nude Neoplasms, Experimental - immunology Recombinant Proteins - metabolism Streptavidin - analogs & derivatives Streptavidin - metabolism Succinates - chemistry Tissue Distribution |
title | Streptavidin in Antibody Pretargeting. 3. Comparison of Biotin Binding and Tissue Localization of 1,2-Cyclohexanedione and Succinic Anhydride Modified Recombinant Streptavidin |
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