The structure and mechanical properties of the proteins of lamprey cartilage

Green, Ellen M.; Winlove, C. Peter

doi:10.1002/bip.22583

Cited by 5 publications

(3 citation statements)

References 53 publications

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“…In particular, confined β‐sheet structures, in some cases semicrystalline blocks of nanometer dimensions as few as five strands of eight amino acids each, reinforce polymer chain networks of diverse structural proteins that are separated by many millions of years of evolution. This general “blueprint” for design holds for silkworm and spider dragline silks, lamprin (a lamprey cartilage protein), and suckerin proteins (forming squid sucker ring teeth), as well as various insect cuticle proteins . A higher proportion of structured segments, commensurate with a reduction in proline residue content, typically correlates with greater material stiffness …”

Section: Discussionmentioning

confidence: 99%

Contribution of domain 30 of tropoelastin to elastic fiber formation and material elasticity

et al. 2016

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Elastin is a fibrous structural protein of the extracellular matrix that provides reversible elastic recoil to vertebrate tissues such as arterial vessels, lung, and skin. The elastin monomer, tropoelastin, contains a large proportion of intrinsically disordered and flexible hydrophobic sequences that collectively are responsible for the initial phase separation of monomers during assembly, and are essential for driving elastic recoil. While structural disorder of hydrophobic sequences is controlled by a high proline and glycine residue composition, hydrophobic domain 30 of human tropoelastin is atypically proline-poor, and forms β-sheet amyloid-like fibrils as an individual peptide. We explored the contribution of confined regions of secondary structure at the location of domain 30 in human tropoelastin to fiber assembly and mechanical properties using a set of mutations designed to inhibit or enhance the propensity of β-sheet formation at this location. Our data support a dual role for confined β-sheet secondary structure in domain 30 of tropoelastin in guiding the formation of fibers, and as a determinant of stiffness and viscoelastic properties of cross-linked materials. Together, these results suggest a mechanism for specificity in fiber assembly, and elucidate structure-function relationships for the rational design of elastomeric biomaterials with defined mechanical properties.

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Section: Discussionmentioning

confidence: 99%

Contribution of domain 30 of tropoelastin to elastic fiber formation and material elasticity

et al. 2016

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“…Proline‐poor spider silks rich in β‐sheet are stiffer than proline‐rich silks . Moreover, a β‐sheet‐forming GGLGY repeat of eggshell chorion and lamprin (a lamprey cartilage protein) contributes to the stiffness of these structural proteins …”

Section: Discussionmentioning

confidence: 99%

Proline‐poor hydrophobic domains modulate the assembly and material properties of polymeric elastin

et al. 2015

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Elastin is a self-assembling extracellular matrix protein that provides elasticity to tissues. For entropic elastomers such as elastin, conformational disorder of the monomer building block, even in the polymeric form, is essential for elastomeric recoil. The highly hydrophobic monomer employs a range of strategies for maintaining disorder and flexibility within hydrophobic domains, particularly involving a minimum compositional threshold of proline and glycine residues. However, the native sequence of hydrophobic elastin domain 30 is uncharacteristically proline-poor and, as an isolated polypeptide, is susceptible to formation of amyloid-like structures comprised of stacked β-sheet. Here we investigated the biophysical and mechanical properties of multiple sets of elastin-like polypeptides designed with different numbers of proline-poor domain 30 from human or rat tropoelastins. We compared the contributions of these proline-poor hydrophobic sequences to self-assembly through characterization of phase separation, and to the tensile properties of cross-linked, polymeric materials. We demonstrate that length of hydrophobic domains and propensity to form β-structure, both affecting polypeptide chain flexibility and cross-link density, play key roles in modulating elastin mechanical properties. This study advances the understanding of elastin sequence-structure-function relationships, and provides new insights that will directly support rational approaches to the design of biomaterials with defined suites of mechanical properties.

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“…Depending on its origin, resilin has a consensus repeat sequences of GGRPSDSYGAPGGGN or AQTPSSQYGAP[36,84]. Lamprin (GGLGX)[85], the most important protein in lamprey cartilage, has been shown to exhibit elastomeric properties[86]. The high molecular weight (HMW) subunits of wheat gluten are seed storage proteins that store essential nutrients such as carbon, nitrogen and sulfur for growth of seedlings.…”

Section: Other Elastomeric Polymers With Idp Characteristicsmentioning

confidence: 99%

Elastin‐like polypeptides as models of intrinsically disordered proteins

2015

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Elastin-like polypeptides (ELPs) are a class of stimuli-responsive biopolymers inspired by the intrinsically disordered domains of tropoelastin that are composed of repeats of the VPGXG pentapeptide motif, where X is a “guest residue”. They undergo a reversible, thermally triggered lower critical solution temperature (LCST) phase transition, which has been utilized for a variety of applications including protein purification, affinity capture, immunoassays, and drug delivery. ELPs have been extensively studied as protein polymers and as biomaterials, but their relationship to other disordered proteins has heretofore not been established. The biophysical properties of ELPs that lend them their unique material behavior are similar to the properties of many intrinsically disordered proteins (IDP). Their low sequence complexity, phase behavior, and elastic properties make them an interesting “minimal” artificial IDP, and the study of ELPs can hence provide insights into the behavior of other more complex IDPs. Motivated by this emerging realization of the similarities between ELPs and IDPs, this review discusses the biophysical properties of ELPs, their biomedical utility, and their relationship to other disordered polypeptide sequences.

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The structure and mechanical properties of the proteins of lamprey cartilage

Cited by 5 publications

References 53 publications

Contribution of domain 30 of tropoelastin to elastic fiber formation and material elasticity

Contribution of domain 30 of tropoelastin to elastic fiber formation and material elasticity

Proline‐poor hydrophobic domains modulate the assembly and material properties of polymeric elastin

Elastin‐like polypeptides as models of intrinsically disordered proteins

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