Biopolymers and biomaterials based on elastomeric proteins

Martino, M; Perri, Tiziana; Tamburro, Antonio Mario

doi:10.1002/1616-5195(200209)2:7<319::aid-mabi319>3.0.co;2-l

Cited by 56 publications

(48 citation statements)

References 78 publications

(127 reference statements)

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“…Only (Lys-Gly-Gly-Val-Gly) n , and (Orn-Gly-Gly-Orn-Gly) n , both polydisperse polymers up to 14 kDa, were intermolecularly crosslinked either by glutaraldehyde and/or by the succinimidyl ester of glutaric acid to obtain biomaterials [169]. Although structural analysis was performed, mechanical and biocompatibility studies are lacking.…”

Section: Elastin-like Polypeptidessupporting

confidence: 44%

Elastin as a biomaterial for tissue engineering

et al. 2007

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Section: Elastin-like Polypeptidessupporting

confidence: 44%

Elastin as a biomaterial for tissue engineering

et al. 2007

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“…36,37 In order to compare our observations with available NMR data, we calculated the torsion angles for each type of amino acid (Val1, Pro2, Gly3, Val4, and Gly5) in (VPGVG) 18 at low (290 K) and high (350 K) temperatures ( Figure 4). We compare our results to the SS-NMR data for the VPGVG segment in (VPGVG) 3 37 and [(VPGVG) 4 (VVPGKG) 39 ] 31 obtained by Hong et al, and the SS-NMR data for the middle segment in (VPGVG) 6 34 obtained by Ohgo et al These studies indicate a significant structural heterogeneity and neither study supported the torsion angles of the β-spiral. 33 Although there is a reasonable agreement between these studies on the overall structural propensities of the VPGVG subunit, the observed differences are primarily in the torsion angles for the valine residues in the VPGVG repeat unit.…”

Section: ■ Resultsmentioning

confidence: 48%

“…31,34 The conformational state of an ELP below its transition temperature was also elucidated by CD spectroscopy, which showed a significant amount of type-II β-turns below the LCST. 35 In addition, a study of (GVGVP) 6 by Gross et al 36 suggested that the polypeptide could adopt a β-sheet structure instead of a β-spiral in the folded state. A solid-state NMR study by Yao and Hong 37 suggested that Urry's model missed the more populated distorted β-strand structure.…”

Section: ■ Introductionmentioning

confidence: 48%

Molecular Description of the LCST Behavior of an Elastin-Like Polypeptide

Quiroz

Hall³

et al. 2014

Biomacromolecules

161

212

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Elastin-like polypeptides (ELPs) with the repeat sequence of VPGVG are widely used as a model system for investigation of lower critical solution temperature (LCST) transition behavior. In this paper, the effect of temperature on the structure, dynamics and association of (VPGVG) 18 in aqueous solution is investigated using atomistic molecular dynamics simulations. Our simulations show that as the temperature increases the ELP backbones undergo gradual conformational changes, which are attributed to the formation of more ordered secondary structures such as β-strands. In addition, increasing temperature changes the hydrophobicity of the ELP by exposure of hydrophobic valine-side chains to the solvent and hiding of proline residues. Based on our simulations, we conclude that the transition behavior of (VPGVG) 18 can be attributed to a combination of thermal disruption of the water network that surrounds the polypeptide, reduction of solvent accessible surface area of the polypeptide, and increase in its hydrophobicity. Simulations of the association of two (VPGVG) 18 molecules demonstrated that the observed gradual changes in the structural properties of the single polypeptide chain are enough to cause the aggregation of polypeptides above the LCST. These results lead us to propose that the LCST phase behavior of poly(VPGVG) is a collective phenomenon that originates from the correlated gradual changes in single polypeptide structure and the abrupt change in properties of hydration water around the peptide and is a result of a competition between peptide−peptide and peptide−water interactions. This is a computational study of an important intrinsically disordered peptide system that provides an atomic-level description of structural features and interactions that are relevant in the LCST phase behavior.

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“…The radically different approach in the methodology utilized to produce these polymers causes that still today a limited number of research groups and companies have done the effort to make this transition. Among those pioneer groups, the main interest has been mainly concentrated in two major polymer families; spider silk-like polymers (Shao and Vollrath 2002) and elastin-like polymers (''ELPs'') (Urry et al 1993;Panitch et al 1999;Chilkoti et al 2002;Martino et al 2002;Rodríguez-Cabello et al 2005) although some other interesting protein polymers have been also addressed.…”

Section: Genetic Engineering Of Protein-based Polymers (Gepbps)mentioning

confidence: 43%

“…A wide variety of polymers have been (bio)synthesized with a general formula (VPGXG), where X represents any natural or modified amino acid (Urry 2005;Martino et al 2002) with the exception of L-proline. All the polymers with that general formula that can be found in the literature are functional; i.e., all show a smart behavior.…”

Section: Elastin-like Polymersmentioning

confidence: 44%

Tailored recombinant elastin-like polymers for advanced biomedical and nano(bio)technological applications

et al. 2006

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The genetic engineering of protein-based polymers is a method that enables, in an easy way, the design of complex and highly functional macromolecules. As examples of this approach, different molecular designs are presented, with increasing degree of complexity, showing how the controlled increase in their complexity yields (multi)functional materials with more selected and sophisticated properties. The simplest designs show interesting properties already, but the adequate introduction of given chemical functions along the polymer chain provides an opportunity to expand the range of properties to enhanced smart behavior and self-assembly. Finally, examples are given where those molecular designs further incorporate selected bioactivities in order to develop materials for the most cutting edge applications in biomedicine and nano(bio)technology.

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Biopolymers and biomaterials based on elastomeric proteins

Cited by 56 publications

References 78 publications

Elastin as a biomaterial for tissue engineering

Elastin as a biomaterial for tissue engineering

Molecular Description of the LCST Behavior of an Elastin-Like Polypeptide

Tailored recombinant elastin-like polymers for advanced biomedical and nano(bio)technological applications

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