Self-assembly polypeptide

Belhngham, C.M., Lillie, M.A., Gosline, J.M., Wright, G.M., Starcher, B.C., Bailey, A.J., Woodhouse, K.A., and Keeley, F.W., Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-hke... 

Keywords Biomaterial Drug delivery Hydrogel Peptide Polypeptide Self-assembly Tissue engineering... 

Sharma N, Top A, Kiick KL et al (2009) One-dimensional gold nanoparticle arrays by electrostatically directed organization using polypeptide self-assembly. Angew Chem Int Ed 48 7078-7082... 

Section 2.1 above). These functional fibrils suggest that designed fibrils can be developed as compatible materials. Toxicology will be a potential issue for all structures that self-assemble on a nanoscale. However, the natural building blocks used to construct protein fibers may increase the biocompatibility of these structures compared to other man-made materials. Polypeptide self-assembly also represents a route for generating ECM-like structures that are not only simpler than their natural equivalents but also easier to prepare. 

Keywords Block copolymers Polypeptides Self-assembly... 

Siddique B, Duhamel J (2011) Effect of polypeptide sequence on polypeptide self-assembly. Langmuir 27 6639-6650... 

Bellingham, C. M., M. A. Lillie, J. M. GosUne, G. M. Wright, B. C. Starcher, A. J. Bailey, K. A. Woodhouse, and F. W. Keeley. 2003. Recombinant human elastin polypeptides self-assemble into biomaterials with elastin-like properties. Biopolymers 70(4) 445-55. 

It was postulated that these polypeptides self-assemble in solution and thus direct the formation of silica structures. These polypeptides were able to form spherical as well as pillar-like structures with TEOS precursor." ... 

Wright E.R., McMillan R., Andrew C.A., Apkarian, R.P., and Conticello, V.P. Thermoplastic elastomer hydrogels via self-assembly of an elastin-mimetic triblock polypeptide, Adv. Func. Mater., 12, 149, 2002. 

Lee T.A.T., Cooper A., Apkarian R.P., and Conticello V.P. Thermo-reversible self-assembly of nano-particles derived from elastin-mimetic polypeptides. Advanced Materials, 12, 1105, 2000. 

Keeley, F.W., Bellingham, C.M., and Woodhouse, K.A., Elastin as a self-organising biomaterial Use of recombinantly expressed human elastin polypeptides as a model system for investigations of structure and self-assembly of elastin, Philos. Trans. R. Soc. Lond. B Biol. Sci., 357, 185-189, 2002. 

To be successful in these applications, it is important that materials can self-assemble into precisely defined structures. Peptide-based polymers have many advantages over conventional synthetic polymers since they are able to hierarchically assemble into stable, ordered conformations [4]. Depending on the substituents of the amino acid side chain, polypeptides are able to adopt a multitude of... 

The way that Pn peptides self-assemble is important for polypeptides and proteins amyloid-type structures are believed to have the same core stmcture, and in fact the propensity to self-assemble in this manner is hypothesized to be a general property of polypeptides [52]. It is therefore unsurprising that systems featuring this motif are common. In recent years, a push towards the use of peptide-based self-assembled materials has led to increasing interest in extending their functionality by derivatising them. 

The first elastomeric protein is elastin, this structural protein is one of the main components of the extracellular matrix, which provides stmctural integrity to the tissues and organs of the body. This highly crosslinked and therefore insoluble protein is the essential element of elastic fibers, which induce elasticity to tissue of lung, skin, and arteries. In these fibers, elastin forms the internal core, which is interspersed with microfibrils [1,2]. Not only this biopolymer but also its precursor material, tropoelastin, have inspired materials scientists for many years. The most interesting characteristic of the precursor is its ability to self-assemble under physiological conditions, thereby demonstrating a lower critical solution temperature (LCST) behavior. This specific property has led to the development of a new class of synthetic polypeptides that mimic elastin in its composition and are therefore also known as elastin-like polypeptides (ELPs). 

This coacervation process forms the basis for the self-assembly, which takes place prior to the crosslinking. The assembly of tropoelastin is based on an ordering process, in which the polypeptides are converted from a state with little order to a more structured conformation [8]. The insoluble elastic fiber is formed via the enzymatic crosslinking of tropoelastin (described in Sect. 2.1). Various models have been proposed to explain the mechanism of elasticity of the elastin fibers. 

Self-Assembled Polypeptide and Polypeptide Hybrid Vesicles From Synthesis to Application... 

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