Comparative structures and properties of elastic proteins

Tatham, Arthur S.; Shewry, Peter R.

doi:10.1098/rstb.2001.1031

Cited by 84 publications

(47 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In particular the length of the repeat in the αC connector region varies from a low in chicken fibrinogen, which has no repeat, to a high in lamprey fibrinogen, which has over 20 repeats of 18 residues (55). Of special note, the amino acid content of the tandem repeat within all αC connectors is intriguingly reminiscent of those in the repeat sequences in elastin, resilin, and spider-silk (56). If the αC region or the repeat region is important, then the fibrin fibers from different species would have different mechanical properties.…”

Section: The αC Regionsmentioning

confidence: 99%

The molecular origins of the mechanical properties of fibrin

Falvo¹,

Gorkun²,

Lord³

2010

Biophysical Chemistry

View full text Add to dashboard Cite

When normal blood circulation is compromised by damage to vessel walls, clots are formed at the site of injury. These clots prevent bleeding and support wound healing. To sustain such physiological functions, clots are remarkably extensible and elastic. Fibrin fibers provide the supporting framework of blood clots, and the properties of these fibers underlie the mechanical properties of clots. Recent studies, which examined individual fibrin fibers or cylindrical fibrin clots, have shown that the mechanical properties of fibrin depend on the mechanical properties of the individual fibrin monomers. Within the fibrin monomer, three structures could contribute to these properties: the coiled-coil connectors the folded globular nodules and the relatively unstructured αC regions. Experimental data suggest that each of these structures contributes. Here we review the recent work with a focus on the molecular origins of the remarkable biomechanical properties of fibrin clots.

show abstract

Section: The αC Regionsmentioning

confidence: 99%

The molecular origins of the mechanical properties of fibrin

Falvo¹,

Gorkun²,

Lord³

2010

Biophysical Chemistry

View full text Add to dashboard Cite

show abstract

“…Therefore, this study presents a rational approach to the structure of abductin based on conformational studies carried out on synthetic repeating sequences strictly mimicking that proved to be successful for many elastomeric proteins, [12] such as elastin, [13] titin, [14] and flagelliform silk proteins. [15] Further rationale for this ''reductionist'' approach lies in the considerations, demonstrated to be valid for tropoelastin, [16][17][18][19] that elastomeric proteins are characterized by autonomous repeating sequences whose structure is almost independent of the remaining parts of the molecules.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of and Structural Studies on Repeating Sequences of Abductin

Bochicchio

Jimenez-Oronoz

Pepe

et al. 2005

Macromolecular Bioscience

View full text Add to dashboard Cite

Little data exist on the structure and function of compressible elastomeric proteins such as abductin. An understanding of the underlying structural features of these proteins may lead to the development of a new class of highly tailored "compressible" hydrogels. To that effect, in this work, the structure of abductin was investigated by means of studies on several synthetic peptides corresponding to the most frequent sequences of abductin. In particular, the 10 amino acid abductin peptide sequence FGGMGGGNAG, tandem repeated in the protein, and two related 25 and 40 amino acid polypeptides were synthesized. These peptides were studied with regard to secondary structure, self-assembly, and polymer morphology. The results obtained with these peptides allow us to propose a preliminary structure-elasticity relationship for abductin not dissimilar from that currently accepted for elastin.A possible mechanism of elasticity relating abductin to elastin.

show abstract

“…This sequence has been the most characterized building block of elastin-like polypeptides (ELPs), 82,83 but other consensus sequences of ELPs such as VPGG, VPAXG, IPAXG, and APGVGV provide the ability to vary the mechanical properties of the materials. 84,85 Resilin, well-known for its extremely high resilience, is a structural component directly related to the mechanics of insect flight, 86 jumping, 87 walking, 88 and phonation. 89 For resilin-like polypeptides (RLPs), a 15-residue repeat sequence GGRPSDSYGAPGGGN derived from the exon I region of proresilin is the most widely used repeat motif.…”

Section: Amorphous Artificially Engineered Protein Gelsmentioning

confidence: 99%

Physics of engineered protein hydrogels

Kim

Tang

Olsen

2013

J Polym Sci B Polym Phys

View full text Add to dashboard Cite

Artificially engineered proteins and synthetic polypeptides have attracted widespread interest as building blocks for polymer hydrogels. The biophysical properties of the proteins, such as molecular recognition abilities, folded chain structures, and sequence-dependent thermodynamic behavior, enable advances in functional, responsive, and tunable gels. This review discusses the design of polymer hydrogels that incorporate protein domains, highlighting new challenges in polymer physics that are presented by this emerging class of materials. Five types of engineered protein hydrogels are discussed: (a) physically associating protein polymer gels, (b) amorphous artificially engineered protein networks, (c) engineered proteins with crystalline domains, (d) stretchable protein tertiary structures in gels, and (e) protein gels with biological recognition properties. The physics of the protein component and the physical properties of the resulting hydrogels are summarized, illustrating how advances in understanding these systems are leading to exciting novel biofunctional hydrogels.

show abstract

Comparative structures and properties of elastic proteins

Cited by 84 publications

References 46 publications

The molecular origins of the mechanical properties of fibrin

The molecular origins of the mechanical properties of fibrin

Synthesis of and Structural Studies on Repeating Sequences of Abductin

Physics of engineered protein hydrogels

Contact Info

Product

Resources

About