Document Detail


Recombinamers: combining molecular complexity with diverse bioactivities for advanced biomedical and biotechnological applications.
MedLine Citation:
PMID:  21072696     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
The rapid development of polymer science has led to literally thousands of different monomers and an almost endless number of possibilities arising from their combination. The most promising strategy to date has been to consider natural products as macromolecules that provide the best option for obtaining functional materials. Proteins, with their high levels of complexity and functionality, are one of the best examples of this approach. In addition, the development of genetic engineering has permitted the design and highly controlled synthesis of proteinaceous materials with complex and advanced functionalities. Elastin-like recombinamers (ELRs) are presented herein as an example of an extraordinary convergence of different properties that is not found in any other synthetic polymer system. These materials are highly biocompatible, stimuli-responsive, show unusual self-assembly properties, and can incorporate bioactive domains and other functionalities along the polypeptide chain. These attributes are an important factor in the development of biomedical and biotechnological applications such as tissue engineering, drug delivery, purification of recombinant proteins, biosensors or stimuli-responsive surfaces.
Authors:
José Carlos Rodríguez-Cabello; María Pierna; Alicia Fernández-Colino; Carmen García-Arévalo; Francisco Javier Arias
Related Documents :
15737536 - Microencapsulation peptide and protein drugs delivery system.
20857356 - Detecting protein-small molecule interactions using fluorous small-molecule microarrays.
12062966 - Towards quantitative assays with peptide chips: a surface engineering approach.
24260366 - Profiling antibody responses to infections by chlamydia abortus enables identification...
8963446 - Distribution of components of the snare complex in relation to transmitter release site...
16415296 - Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Advances in biochemical engineering/biotechnology     Volume:  125     ISSN:  1616-8542     ISO Abbreviation:  Adv. Biochem. Eng. Biotechnol.     Publication Date:  2011  
Date Detail:
Created Date:  2011-08-05     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8307733     Medline TA:  Adv Biochem Eng Biotechnol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  145-79     Citation Subset:  IM    
Affiliation:
G.I.R. Bioforge, University of Valladolid, CIBER-BBN, Paseo de Belén 11, Valladolid, Spain, cabello@eis.uva.es.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Single cell analytics: an overview.
Next Document:  Chitin, chitosan and derivatives for wound healing and tissue engineering.