English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/19117
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
DC FieldValueLanguage
dc.contributor.authorAlmiñana, Nuria-
dc.contributor.authorAlsina, M. Asunción-
dc.contributor.authorOrtiz, A.-
dc.contributor.authorReig Isart, Francesca-
dc.date.accessioned2009-11-27T13:41:46Z-
dc.date.available2009-11-27T13:41:46Z-
dc.date.issued2004-11-16-
dc.identifier.citationColloids and Surfaces A: Physicochemical and Engineering Aspects 249 (1-3): 19-24 (2004)en_US
dc.identifier.issn0927-7757-
dc.identifier.urihttp://hdl.handle.net/10261/19117-
dc.description6 pages, 6 figures, 1 table.-- Printed version published Nov 30, 2004.-- Issue title: "1st International Meeting on Applied Physics" (Badajoz, Spain, Oct 15-18, 2003).en_US
dc.description.abstractSIKVAV is an active site of laminin involved in different physiological and pathological functions, including neurite outgrowth, angiogenesis and tumor development. In this paper, we report the synthesis of the retro (reverse L-amino acid order) and retro-enantio (reverse D-amino acid order) analogues of the SIKVAV peptide, in order to compare their physicochemical characteristics. When a linear peptide is synthesized with D-amino acids (enantio modification) assembled in the reverse order (retro modification), it presents side chains orientation very similar to that in the original structure. Such peptidomimetic approach provides peptides with a higher metabolic stability. However, there is no evidence if this peptidomimetic approach also maintains the physicochemical characteristics of the original sequence. Surface activity, compression isotherms, kinetic penetration into L-α-Dipalmitoylphosphatidylcholine and L-α-phosphatidylcholine monolayers and miscibility with L-α-Dipalmitoyl-phosphatidylcholine at different molar ratios were determined for each peptide. Results show that either retro or retro-enantio modifications enhance the hydrophilic character of the SIKVAV sequence.en_US
dc.description.sponsorshipThis work was financial supported by a SAF 97-0174 project and Núria Almiñana was recipient of a grant from the Ministry of Science and Technology from the Spanish Government.en_US
dc.format.extent22195 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.rightsclosedAccessen_US
dc.subjectSIKVAVen_US
dc.subjectRetro and retro-enantio peptidesen_US
dc.subjectSurface activityen_US
dc.subjectCompression isothermsen_US
dc.subjectKinetic penetrationen_US
dc.subjectMiscibilityen_US
dc.titleComparative physicochemical study of SIKVAV peptide and its retro and retro-enantio analoguesen_US
dc.typeartículoen_US
dc.identifier.doi10.1016/j.colsurfa.2004.08.041-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.colsurfa.2004.08.041en_US
Appears in Collections:(IQAC) Artículos
Files in This Item:
There are no files associated with this item.
Show simple item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.