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Titre du document / Document title

Polypeptide hydrogels via a unique assembly mechanism

Auteur(s) / Author(s)

DEMING Timothy J. (1) ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

(1) Department of Bioengineering, University of California, Los Angeles, CA 90095, ETATS-UNIS

Résumé / Abstract

There is a long history of man's use of materials derived from peptides and proteins. These natural materials possess sophisticated mechanisms of nanoscale self assembly, which have inspired the design of many synthetic and biosynthetic amino-acid based materials. These materials are attractive since they can have exceptional properties, environmental responsive behavior, biological activity, and can be metabolized. With all of their complexity, peptides and proteins rely primarily on two fundamental modes of self assembly: association of β-strands and the coiling of helices. In this context, a class of recently synthesized and characterized polypeptide materials are reviewed here, which were found to self-assemble by a fundamentally different process. This new mode of assembly was found to give rise to polypeptide hydrogels with a unique combination of properties (e.g. heat stability and injectability) making them attractive for applications in foods, personal care products, and medicine.

Revue / Journal Title

Journal of material chemistry    ISSN  0959-9428 

Source / Source

2005, vol. 15, no22, pp. 28-35 [8 page(s) (article)] (20 ref.)

Langue / Language

Anglais

Editeur / Publisher

Royal Society of Chemistry, Cambridge, ROYAUME-UNI  (1991) (Revue)

Mots-clés anglais / English Keywords

Stability

;

Vibrational modes

;

Reviews

;

Biological activity

;

Self-assembly

;

Nanostructures

;

Proteins

;

Peptides

;

Mots-clés français / French Keywords

63

;

Stabilité

;

Mode vibration

;

Article synthèse

;

Activité biologique

;

Autoassemblage

;

Nanostructure

;

Protéine

;

Peptide

;

Mots-clés espagnols / Spanish Keywords

Actividad biológica

;

Localisation / Location

INIST-CNRS, Cote INIST : 22603, 35400013805388.0140

Nº notice refdoc (ud4) : 16870324



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