Polyphosphazene Polyelectrolytes: A Link between the Formation of Noncovalent Complexes with Antigenic Proteins and Immunostimulating Activity
Polyphosphazene polyelectrolytes are potent immunostimulants. Their in vivo performance has been demonstrated for various antigens in a number of animal models. To improve understanding of the mechanism of action, we performed a comparative study in a model system: bovine serum albumin, BSA−poly[di...
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Veröffentlicht in: | Biomacromolecules 2005-05, Vol.6 (3), p.1375-1379 |
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description | Polyphosphazene polyelectrolytes are potent immunostimulants. Their in vivo performance has been demonstrated for various antigens in a number of animal models. To improve understanding of the mechanism of action, we performed a comparative study in a model system: bovine serum albumin, BSA−poly[di(carboxylatophenoxy)phosphazene], PCPP, in vitro and in vivo. Multi-angle laser light scattering (MALLS) and size-exclusion HPLC methods were used to investigate polyphosphazene−protein formulations in an attempt to establish correlations between their physicochemical behavior and immunostimulating activity. These studies revealed the formation of water-soluble noncovalent protein−polymer complexes in the system. It was shown that both the amount of bound protein and the complex conformation could play an important role in the in vivo performance of the polyphosphazene polyelectrolytes. |
doi_str_mv | 10.1021/bm049329t |
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Their in vivo performance has been demonstrated for various antigens in a number of animal models. To improve understanding of the mechanism of action, we performed a comparative study in a model system: bovine serum albumin, BSA−poly[di(carboxylatophenoxy)phosphazene], PCPP, in vitro and in vivo. Multi-angle laser light scattering (MALLS) and size-exclusion HPLC methods were used to investigate polyphosphazene−protein formulations in an attempt to establish correlations between their physicochemical behavior and immunostimulating activity. These studies revealed the formation of water-soluble noncovalent protein−polymer complexes in the system. 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Their in vivo performance has been demonstrated for various antigens in a number of animal models. To improve understanding of the mechanism of action, we performed a comparative study in a model system: bovine serum albumin, BSA−poly[di(carboxylatophenoxy)phosphazene], PCPP, in vitro and in vivo. Multi-angle laser light scattering (MALLS) and size-exclusion HPLC methods were used to investigate polyphosphazene−protein formulations in an attempt to establish correlations between their physicochemical behavior and immunostimulating activity. These studies revealed the formation of water-soluble noncovalent protein−polymer complexes in the system. It was shown that both the amount of bound protein and the complex conformation could play an important role in the in vivo performance of the polyphosphazene polyelectrolytes.</description><subject>Adjuvants, Immunologic - blood</subject><subject>Adjuvants, Immunologic - chemistry</subject><subject>Animals</subject><subject>Applied sciences</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Chemistry, Pharmaceutical</subject><subject>Electrolytes</subject><subject>Exact sciences and technology</subject><subject>Immunomodulators</subject><subject>Inorganic and organomineral polymers</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Organophosphorus Compounds - blood</subject><subject>Organophosphorus Compounds - chemistry</subject><subject>Pharmacology. Drug treatments</subject><subject>Physicochemistry of polymers</subject><subject>Polymers - chemistry</subject><subject>Properties and characterization</subject><subject>Protein Binding - physiology</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Serum Albumin, Bovine - metabolism</subject><issn>1525-7797</issn><issn>1526-4602</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0btuFDEUBuARApELFLwAcgNSigF7fJuhW60IRFpBCqhHHs9x1sGXwfYkLBUtJa_IkzAhK0KBROVj6Tu_Jf9V9YTgFwQ35OXgMeto05V71SHhjaiZwM393zOvpezkQXWU8yXGuKOMP6wOCG-lpJwfVj_Oo9tN25inrfoKAdDNHRzokpahQH7189t3tEIbGz6hAco1QEBlC-g0Jq-KjQFFg97FoOOVchAKWkc_OfgCGV3bskWrUOwFBKvReYoFbMhIhRGdeT-HmIv1s1tiwgVa6WKvbNk9qh4Y5TI83p_H1cfT1x_Wb-vN-zdn69WmVlSyUlNGOi3kiCknAjNFdSdaLszYsnHoMB_MaLRhRhjFu07LYcRaStnyZtlbluhx9fw2d0rx8wy59N5mDc6pAHHOvZAtFlSw_0IimWg4aRZ4cgt1ijknMP2UrFdp1xPc3xTV_ylqsU_3ofPgYbyT-2YW8GwPVNbKmaSCtvnOiZYJ1v7llM79ZZxTWD7tHw_-AiNQquA</recordid><startdate>20050501</startdate><enddate>20050501</enddate><creator>Andrianov, Alexander K</creator><creator>Marin, Alexander</creator><creator>Roberts, Bryan E</creator><general>American Chemical Society</general><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20050501</creationdate><title>Polyphosphazene Polyelectrolytes: A Link between the Formation of Noncovalent Complexes with Antigenic Proteins and Immunostimulating Activity</title><author>Andrianov, Alexander K ; Marin, Alexander ; Roberts, Bryan E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a374t-3419c67d0351604a3c96856fd84db905bfdfcf4f6fa599c7bd0c77785219c0353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adjuvants, Immunologic - blood</topic><topic>Adjuvants, Immunologic - chemistry</topic><topic>Animals</topic><topic>Applied sciences</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Chemistry, Pharmaceutical</topic><topic>Electrolytes</topic><topic>Exact sciences and technology</topic><topic>Immunomodulators</topic><topic>Inorganic and organomineral polymers</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Organophosphorus Compounds - blood</topic><topic>Organophosphorus Compounds - chemistry</topic><topic>Pharmacology. Drug treatments</topic><topic>Physicochemistry of polymers</topic><topic>Polymers - chemistry</topic><topic>Properties and characterization</topic><topic>Protein Binding - physiology</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Serum Albumin, Bovine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Andrianov, Alexander K</creatorcontrib><creatorcontrib>Marin, Alexander</creatorcontrib><creatorcontrib>Roberts, Bryan E</creatorcontrib><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biomacromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Andrianov, Alexander K</au><au>Marin, Alexander</au><au>Roberts, Bryan E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Polyphosphazene Polyelectrolytes: A Link between the Formation of Noncovalent Complexes with Antigenic Proteins and Immunostimulating Activity</atitle><jtitle>Biomacromolecules</jtitle><addtitle>Biomacromolecules</addtitle><date>2005-05-01</date><risdate>2005</risdate><volume>6</volume><issue>3</issue><spage>1375</spage><epage>1379</epage><pages>1375-1379</pages><issn>1525-7797</issn><eissn>1526-4602</eissn><abstract>Polyphosphazene polyelectrolytes are potent immunostimulants. Their in vivo performance has been demonstrated for various antigens in a number of animal models. To improve understanding of the mechanism of action, we performed a comparative study in a model system: bovine serum albumin, BSA−poly[di(carboxylatophenoxy)phosphazene], PCPP, in vitro and in vivo. Multi-angle laser light scattering (MALLS) and size-exclusion HPLC methods were used to investigate polyphosphazene−protein formulations in an attempt to establish correlations between their physicochemical behavior and immunostimulating activity. These studies revealed the formation of water-soluble noncovalent protein−polymer complexes in the system. It was shown that both the amount of bound protein and the complex conformation could play an important role in the in vivo performance of the polyphosphazene polyelectrolytes.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15877355</pmid><doi>10.1021/bm049329t</doi><tpages>5</tpages></addata></record> |
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subjects | Adjuvants, Immunologic - blood Adjuvants, Immunologic - chemistry Animals Applied sciences Biological and medical sciences Cattle Chemistry, Pharmaceutical Electrolytes Exact sciences and technology Immunomodulators Inorganic and organomineral polymers Medical sciences Mice Mice, Inbred BALB C Organophosphorus Compounds - blood Organophosphorus Compounds - chemistry Pharmacology. Drug treatments Physicochemistry of polymers Polymers - chemistry Properties and characterization Protein Binding - physiology Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism |
title | Polyphosphazene Polyelectrolytes: A Link between the Formation of Noncovalent Complexes with Antigenic Proteins and Immunostimulating Activity |
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