New transport peptides broaden the horizon of applications for peptidic pharmaceuticals
Protein transduction domains (PTDs) have proven to be an invaluable tool to transduce a wide variety of cargo's including peptides across the plasma membrane and into intact tissue. The PTDs are able to deliver biologically active molecules both in vitro and in vivo. This study describes many n...
Gespeichert in:
| Veröffentlicht in: | Molecular diversity 2004, Vol.8 (2), p.101-111 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 111 |
|---|---|
| container_issue | 2 |
| container_start_page | 101 |
| container_title | Molecular diversity |
| container_volume | 8 |
| creator | Langedijk, J P M Olijhoek, T Schut, D Autar, R Meloen, R H |
| description | Protein transduction domains (PTDs) have proven to be an invaluable tool to transduce a wide variety of cargo's including peptides across the plasma membrane and into intact tissue. The PTDs are able to deliver biologically active molecules both in vitro and in vivo. This study describes many new polybasic PTDs of which some are just as potent as the PTDs derived from extracellular RNAses or other published PTDs. Large differences in potency became apparent when the PTDs are coupled to particular cargoes. Therefore, the unique characteristic of a PTD may only become apparent when it is selected for a particular application. Rules for optimization of PTDs for particular applications are now emerging and open the way for a new generation of drug delivery agents. Because fixation artifacts and irreversible membrane binding may cause misinterpretation of the amount of internalization of polybasic peptides, we have developed an enzyme transduction assay based on the intracellular loading of a cell permeable substrate. In this assay, a fluorescent signal is generated by internalized enzyme in intact cells and not by membrane-bound or extracellular enzyme. |
| doi_str_mv | 10.1023/B:MODI.0000025653.26130.ce |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66656419</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>20235919</sourcerecordid><originalsourceid>FETCH-LOGICAL-c373t-ff8833c3437d772951dda57d1971b01f0b1266399442e0313cda48de1dddf4e53</originalsourceid><addsrcrecordid>eNqFkU1r3DAQhkVoaT7avxBEDr15q_FYkpVb8x1Im0tLexNaacw67FquZBPSXx9tshDopUIwgnneEdLD2AmIBYgav5ydfru_uF2I7aqlkrioFaBYeNpjByA1VlLA73fljC1UYAzss8OcH4SAsvED2wdZCwMKDtiv7_TIp-SGPMY08ZHGqQ-U-TJFF2jg04r4Kqb-bxx47Lgbx3Xv3dTHIfMupl2g93xcubRxnuap9Nf5I3vflUKfdvWI_by6_HF-U93dX9-ef72rPGqcqq5rW0SPDeqgdW0khOCkDmA0LAV0Ygm1UmhM09QkENAH17SBCha6hiQesc-vc8cU_8yUJ7vps6f12g0U52yVUlI1YP4L1uVnpXkBT_4BH-KchvIIq2XpC9HqAp2-Qj7FnBN1dkz9xqUnC8JuJdkzu5Vk3yTZF0nWUwkf726YlxsKb9GdFXwG9LuOpw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>751930087</pqid></control><display><type>article</type><title>New transport peptides broaden the horizon of applications for peptidic pharmaceuticals</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Langedijk, J P M ; Olijhoek, T ; Schut, D ; Autar, R ; Meloen, R H</creator><creatorcontrib>Langedijk, J P M ; Olijhoek, T ; Schut, D ; Autar, R ; Meloen, R H</creatorcontrib><description>Protein transduction domains (PTDs) have proven to be an invaluable tool to transduce a wide variety of cargo's including peptides across the plasma membrane and into intact tissue. The PTDs are able to deliver biologically active molecules both in vitro and in vivo. This study describes many new polybasic PTDs of which some are just as potent as the PTDs derived from extracellular RNAses or other published PTDs. Large differences in potency became apparent when the PTDs are coupled to particular cargoes. Therefore, the unique characteristic of a PTD may only become apparent when it is selected for a particular application. Rules for optimization of PTDs for particular applications are now emerging and open the way for a new generation of drug delivery agents. Because fixation artifacts and irreversible membrane binding may cause misinterpretation of the amount of internalization of polybasic peptides, we have developed an enzyme transduction assay based on the intracellular loading of a cell permeable substrate. In this assay, a fluorescent signal is generated by internalized enzyme in intact cells and not by membrane-bound or extracellular enzyme.</description><identifier>ISSN: 1381-1991</identifier><identifier>EISSN: 1573-501X</identifier><identifier>DOI: 10.1023/B:MODI.0000025653.26130.ce</identifier><identifier>PMID: 15209161</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Amino Acid Sequence ; Animals ; beta-Galactosidase - genetics ; beta-Galactosidase - metabolism ; Binding Sites ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cattle ; Cells, Cultured ; Fluorescein-5-isothiocyanate - chemistry ; Fluorescein-5-isothiocyanate - metabolism ; Fluoresceins - chemistry ; Fluoresceins - metabolism ; Fluorescent Dyes - chemistry ; Fluorescent Dyes - metabolism ; Galactosides - chemistry ; Galactosides - metabolism ; Gene Products, tat - genetics ; Gene Products, tat - metabolism ; Heparin - metabolism ; Horseradish Peroxidase - genetics ; Horseradish Peroxidase - metabolism ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Molecular Biology - methods ; Molecular Sequence Data ; Peptide Mapping ; Peptides ; Peptides - analysis ; Peptides - genetics ; Peptides - metabolism ; Protein Engineering - methods ; Protein Structure, Tertiary ; Protein Transport ; Streptavidin - chemistry ; Streptavidin - metabolism ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - metabolism</subject><ispartof>Molecular diversity, 2004, Vol.8 (2), p.101-111</ispartof><rights>Kluwer Academic Publishers 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c373t-ff8833c3437d772951dda57d1971b01f0b1266399442e0313cda48de1dddf4e53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15209161$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Langedijk, J P M</creatorcontrib><creatorcontrib>Olijhoek, T</creatorcontrib><creatorcontrib>Schut, D</creatorcontrib><creatorcontrib>Autar, R</creatorcontrib><creatorcontrib>Meloen, R H</creatorcontrib><title>New transport peptides broaden the horizon of applications for peptidic pharmaceuticals</title><title>Molecular diversity</title><addtitle>Mol Divers</addtitle><description>Protein transduction domains (PTDs) have proven to be an invaluable tool to transduce a wide variety of cargo's including peptides across the plasma membrane and into intact tissue. The PTDs are able to deliver biologically active molecules both in vitro and in vivo. This study describes many new polybasic PTDs of which some are just as potent as the PTDs derived from extracellular RNAses or other published PTDs. Large differences in potency became apparent when the PTDs are coupled to particular cargoes. Therefore, the unique characteristic of a PTD may only become apparent when it is selected for a particular application. Rules for optimization of PTDs for particular applications are now emerging and open the way for a new generation of drug delivery agents. Because fixation artifacts and irreversible membrane binding may cause misinterpretation of the amount of internalization of polybasic peptides, we have developed an enzyme transduction assay based on the intracellular loading of a cell permeable substrate. In this assay, a fluorescent signal is generated by internalized enzyme in intact cells and not by membrane-bound or extracellular enzyme.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>beta-Galactosidase - genetics</subject><subject>beta-Galactosidase - metabolism</subject><subject>Binding Sites</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Fluorescein-5-isothiocyanate - chemistry</subject><subject>Fluorescein-5-isothiocyanate - metabolism</subject><subject>Fluoresceins - chemistry</subject><subject>Fluoresceins - metabolism</subject><subject>Fluorescent Dyes - chemistry</subject><subject>Fluorescent Dyes - metabolism</subject><subject>Galactosides - chemistry</subject><subject>Galactosides - metabolism</subject><subject>Gene Products, tat - genetics</subject><subject>Gene Products, tat - metabolism</subject><subject>Heparin - metabolism</subject><subject>Horseradish Peroxidase - genetics</subject><subject>Horseradish Peroxidase - metabolism</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Molecular Biology - methods</subject><subject>Molecular Sequence Data</subject><subject>Peptide Mapping</subject><subject>Peptides</subject><subject>Peptides - analysis</subject><subject>Peptides - genetics</subject><subject>Peptides - metabolism</subject><subject>Protein Engineering - methods</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>Streptavidin - chemistry</subject><subject>Streptavidin - metabolism</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - metabolism</subject><issn>1381-1991</issn><issn>1573-501X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkU1r3DAQhkVoaT7avxBEDr15q_FYkpVb8x1Im0tLexNaacw67FquZBPSXx9tshDopUIwgnneEdLD2AmIBYgav5ydfru_uF2I7aqlkrioFaBYeNpjByA1VlLA73fljC1UYAzss8OcH4SAsvED2wdZCwMKDtiv7_TIp-SGPMY08ZHGqQ-U-TJFF2jg04r4Kqb-bxx47Lgbx3Xv3dTHIfMupl2g93xcubRxnuap9Nf5I3vflUKfdvWI_by6_HF-U93dX9-ef72rPGqcqq5rW0SPDeqgdW0khOCkDmA0LAV0Ygm1UmhM09QkENAH17SBCha6hiQesc-vc8cU_8yUJ7vps6f12g0U52yVUlI1YP4L1uVnpXkBT_4BH-KchvIIq2XpC9HqAp2-Qj7FnBN1dkz9xqUnC8JuJdkzu5Vk3yTZF0nWUwkf726YlxsKb9GdFXwG9LuOpw</recordid><startdate>2004</startdate><enddate>2004</enddate><creator>Langedijk, J P M</creator><creator>Olijhoek, T</creator><creator>Schut, D</creator><creator>Autar, R</creator><creator>Meloen, R H</creator><general>Springer Nature B.V</general><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>2004</creationdate><title>New transport peptides broaden the horizon of applications for peptidic pharmaceuticals</title><author>Langedijk, J P M ; Olijhoek, T ; Schut, D ; Autar, R ; Meloen, R H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c373t-ff8833c3437d772951dda57d1971b01f0b1266399442e0313cda48de1dddf4e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>beta-Galactosidase - genetics</topic><topic>beta-Galactosidase - metabolism</topic><topic>Binding Sites</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Fluorescein-5-isothiocyanate - chemistry</topic><topic>Fluorescein-5-isothiocyanate - metabolism</topic><topic>Fluoresceins - chemistry</topic><topic>Fluoresceins - metabolism</topic><topic>Fluorescent Dyes - chemistry</topic><topic>Fluorescent Dyes - metabolism</topic><topic>Galactosides - chemistry</topic><topic>Galactosides - metabolism</topic><topic>Gene Products, tat - genetics</topic><topic>Gene Products, tat - metabolism</topic><topic>Heparin - metabolism</topic><topic>Horseradish Peroxidase - genetics</topic><topic>Horseradish Peroxidase - metabolism</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Molecular Biology - methods</topic><topic>Molecular Sequence Data</topic><topic>Peptide Mapping</topic><topic>Peptides</topic><topic>Peptides - analysis</topic><topic>Peptides - genetics</topic><topic>Peptides - metabolism</topic><topic>Protein Engineering - methods</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>Streptavidin - chemistry</topic><topic>Streptavidin - metabolism</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Langedijk, J P M</creatorcontrib><creatorcontrib>Olijhoek, T</creatorcontrib><creatorcontrib>Schut, D</creatorcontrib><creatorcontrib>Autar, R</creatorcontrib><creatorcontrib>Meloen, R H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</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>Molecular diversity</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Langedijk, J P M</au><au>Olijhoek, T</au><au>Schut, D</au><au>Autar, R</au><au>Meloen, R H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New transport peptides broaden the horizon of applications for peptidic pharmaceuticals</atitle><jtitle>Molecular diversity</jtitle><addtitle>Mol Divers</addtitle><date>2004</date><risdate>2004</risdate><volume>8</volume><issue>2</issue><spage>101</spage><epage>111</epage><pages>101-111</pages><issn>1381-1991</issn><eissn>1573-501X</eissn><abstract>Protein transduction domains (PTDs) have proven to be an invaluable tool to transduce a wide variety of cargo's including peptides across the plasma membrane and into intact tissue. The PTDs are able to deliver biologically active molecules both in vitro and in vivo. This study describes many new polybasic PTDs of which some are just as potent as the PTDs derived from extracellular RNAses or other published PTDs. Large differences in potency became apparent when the PTDs are coupled to particular cargoes. Therefore, the unique characteristic of a PTD may only become apparent when it is selected for a particular application. Rules for optimization of PTDs for particular applications are now emerging and open the way for a new generation of drug delivery agents. Because fixation artifacts and irreversible membrane binding may cause misinterpretation of the amount of internalization of polybasic peptides, we have developed an enzyme transduction assay based on the intracellular loading of a cell permeable substrate. In this assay, a fluorescent signal is generated by internalized enzyme in intact cells and not by membrane-bound or extracellular enzyme.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>15209161</pmid><doi>10.1023/B:MODI.0000025653.26130.ce</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1381-1991 |
| ispartof | Molecular diversity, 2004, Vol.8 (2), p.101-111 |
| issn | 1381-1991 1573-501X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66656419 |
| source | MEDLINE; SpringerLink Journals |
| subjects | Amino Acid Sequence Animals beta-Galactosidase - genetics beta-Galactosidase - metabolism Binding Sites Carrier Proteins - genetics Carrier Proteins - metabolism Cattle Cells, Cultured Fluorescein-5-isothiocyanate - chemistry Fluorescein-5-isothiocyanate - metabolism Fluoresceins - chemistry Fluoresceins - metabolism Fluorescent Dyes - chemistry Fluorescent Dyes - metabolism Galactosides - chemistry Galactosides - metabolism Gene Products, tat - genetics Gene Products, tat - metabolism Heparin - metabolism Horseradish Peroxidase - genetics Horseradish Peroxidase - metabolism Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Molecular Biology - methods Molecular Sequence Data Peptide Mapping Peptides Peptides - analysis Peptides - genetics Peptides - metabolism Protein Engineering - methods Protein Structure, Tertiary Protein Transport Streptavidin - chemistry Streptavidin - metabolism Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism |
| title | New transport peptides broaden the horizon of applications for peptidic pharmaceuticals |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T03%3A37%3A30IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=New%20transport%20peptides%20broaden%20the%20horizon%20of%20applications%20for%20peptidic%20pharmaceuticals&rft.jtitle=Molecular%20diversity&rft.au=Langedijk,%20J%20P%20M&rft.date=2004&rft.volume=8&rft.issue=2&rft.spage=101&rft.epage=111&rft.pages=101-111&rft.issn=1381-1991&rft.eissn=1573-501X&rft_id=info:doi/10.1023/B:MODI.0000025653.26130.ce&rft_dat=%3Cproquest_cross%3E20235919%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=751930087&rft_id=info:pmid/15209161&rfr_iscdi=true |