De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins
A new strategy is presented for the designand synthesis of peptides that exhibitice-binding and antifreeze activity. Apennant-type dendrimer polypeptidescaffold combining an α-helical backbonewith four short β-strand branches wassynthesized in solid phase using Fmocchemistry in a divergent approach....
- Autores:
-
Vera Bravo, Ricardo
Scotter, Andrew J.
Davies, Peter
Blanco, Luis Hernando
- Tipo de recurso:
- Article of journal
- Fecha de publicación:
- 2012
- Institución:
- Universidad Nacional de Colombia
- Repositorio:
- Universidad Nacional de Colombia
- Idioma:
- spa
- OAI Identifier:
- oai:repositorio.unal.edu.co:unal/41073
- Acceso en línea:
- https://repositorio.unal.edu.co/handle/unal/41073
http://bdigital.unal.edu.co/31170/
- Palabra clave:
- Rights
- openAccess
- License
- Atribución-NoComercial 4.0 Internacional
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Atribución-NoComercial 4.0 InternacionalDerechos reservados - Universidad Nacional de Colombiahttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Vera Bravo, Ricardo132f698d-4f4f-4732-877f-76632502cf56300Scotter, Andrew J.cfd05817-4616-473f-9eb4-5921f2d824d6300Davies, Peter37be020e-0e45-4eea-a528-d2907188052c300Blanco, Luis Hernando6aeda8d1-47bd-41bb-a201-b7725f2c31e13002019-06-28T09:48:11Z2019-06-28T09:48:11Z2012https://repositorio.unal.edu.co/handle/unal/41073http://bdigital.unal.edu.co/31170/A new strategy is presented for the designand synthesis of peptides that exhibitice-binding and antifreeze activity. Apennant-type dendrimer polypeptidescaffold combining an α-helical backbonewith four short β-strand branches wassynthesized in solid phase using Fmocchemistry in a divergent approach. The51-residue dendrimer was characterizedby reverse phase high performance liquidchromatography, mass spectrometry andcircular dichroism. Each β-strand branchcontained three overlapping TXT aminoacid repeats, an ice-binding motif foundin the ice-binding face of the sprucebudworm (Choristoneura fumiferana)and beetle (Tenebrio molitor) antifreezeproteins. Ice crystals in the presence ofthe polypeptide monomer displayed flat,hexagonal plate morphology, similar tothat produced by weakly active antifreezeproteins. An oxidized dimeric form of thedendrimer polypeptide also produced flathexagonal ice crystals and was capableof inhibiting ice crystal growth upontemperature reduction, a phenomenontermed thermal hysteresis, a definingproperty of antifreeze proteins. Linkageof the pennant-type dendrimer to a trifunctionalcascade-type polypeptideproduced a trimeric macromolecule thatgave flat hexagonal ice crystals withhigher thermal hysteresis activity thanthe dimer or monomer and an ice crystal burst pattern similar to that producedby samples containing insect antifreezeproteins. This macromolecule was alsocapable of inhibiting ice recrystallization.application/pdfspaUniversidad Nacional de Colombiahttp://revistas.unal.edu.co/index.php/rcolquim/article/view/30313Universidad Nacional de Colombia Revistas electrónicas UN Revista Colombiana de QuímicaRevista Colombiana de QuímicaRevista Colombiana de Química; Vol. 41, núm. 1 (2012); 133-151 0120-2804Vera Bravo, Ricardo and Scotter, Andrew J. and Davies, Peter and Blanco, Luis Hernando (2012) De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins. Revista Colombiana de Química; Vol. 41, núm. 1 (2012); 133-151 0120-2804 .De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteinsArtículo de revistainfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85Texthttp://purl.org/redcol/resource_type/ARTORIGINAL30313-109584-1-PB.pdfapplication/pdf699226https://repositorio.unal.edu.co/bitstream/unal/41073/1/30313-109584-1-PB.pdf0d163ee6e606923b4a4851073995d251MD51THUMBNAIL30313-109584-1-PB.pdf.jpg30313-109584-1-PB.pdf.jpgGenerated Thumbnailimage/jpeg8012https://repositorio.unal.edu.co/bitstream/unal/41073/2/30313-109584-1-PB.pdf.jpg688b55cba68ccb837bec11df80febd9fMD52unal/41073oai:repositorio.unal.edu.co:unal/410732023-02-01 23:04:37.872Repositorio Institucional Universidad Nacional de Colombiarepositorio_nal@unal.edu.co |
| dc.title.spa.fl_str_mv |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| title |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| spellingShingle |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| title_short |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| title_full |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| title_fullStr |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| title_full_unstemmed |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| title_sort |
De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins |
| dc.creator.fl_str_mv |
Vera Bravo, Ricardo Scotter, Andrew J. Davies, Peter Blanco, Luis Hernando |
| dc.contributor.author.spa.fl_str_mv |
Vera Bravo, Ricardo Scotter, Andrew J. Davies, Peter Blanco, Luis Hernando |
| description |
A new strategy is presented for the designand synthesis of peptides that exhibitice-binding and antifreeze activity. Apennant-type dendrimer polypeptidescaffold combining an α-helical backbonewith four short β-strand branches wassynthesized in solid phase using Fmocchemistry in a divergent approach. The51-residue dendrimer was characterizedby reverse phase high performance liquidchromatography, mass spectrometry andcircular dichroism. Each β-strand branchcontained three overlapping TXT aminoacid repeats, an ice-binding motif foundin the ice-binding face of the sprucebudworm (Choristoneura fumiferana)and beetle (Tenebrio molitor) antifreezeproteins. Ice crystals in the presence ofthe polypeptide monomer displayed flat,hexagonal plate morphology, similar tothat produced by weakly active antifreezeproteins. An oxidized dimeric form of thedendrimer polypeptide also produced flathexagonal ice crystals and was capableof inhibiting ice crystal growth upontemperature reduction, a phenomenontermed thermal hysteresis, a definingproperty of antifreeze proteins. Linkageof the pennant-type dendrimer to a trifunctionalcascade-type polypeptideproduced a trimeric macromolecule thatgave flat hexagonal ice crystals withhigher thermal hysteresis activity thanthe dimer or monomer and an ice crystal burst pattern similar to that producedby samples containing insect antifreezeproteins. This macromolecule was alsocapable of inhibiting ice recrystallization. |
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2012 |
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2012 |
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2019-06-28T09:48:11Z |
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2019-06-28T09:48:11Z |
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Artículo de revista |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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info:eu-repo/semantics/article |
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http://purl.org/coar/resource_type/c_6501 |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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Text |
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http://purl.org/redcol/resource_type/ART |
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publishedVersion |
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https://repositorio.unal.edu.co/handle/unal/41073 |
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http://bdigital.unal.edu.co/31170/ |
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https://repositorio.unal.edu.co/handle/unal/41073 http://bdigital.unal.edu.co/31170/ |
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spa |
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spa |
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http://revistas.unal.edu.co/index.php/rcolquim/article/view/30313 |
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Universidad Nacional de Colombia Revistas electrónicas UN Revista Colombiana de Química Revista Colombiana de Química |
| dc.relation.ispartofseries.none.fl_str_mv |
Revista Colombiana de Química; Vol. 41, núm. 1 (2012); 133-151 0120-2804 |
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Vera Bravo, Ricardo and Scotter, Andrew J. and Davies, Peter and Blanco, Luis Hernando (2012) De novo design and synthesis of an ice-binding, dendrimeric, polypeptide based on insect antifreeze proteins. Revista Colombiana de Química; Vol. 41, núm. 1 (2012); 133-151 0120-2804 . |
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Derechos reservados - Universidad Nacional de Colombia |
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http://purl.org/coar/access_right/c_abf2 |
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Atribución-NoComercial 4.0 Internacional |
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info:eu-repo/semantics/openAccess |
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