doi: 10.1016/j.ajhg.2009.09.013. The cross-linking domains are defined by lysines, which are responsible for the formation of durable bi-, tri-, and tetrafunctional cross-links within mature elastin. All authors contributed to writing and editing the review. Matrix Biol. Matrix Biol. Elastin is one of the most abundant proteins in your body. Chem. Acta 761, 1722. Four days after a heart attack, purified tropoelastin was injected into the heart. In vitro elastogenesis: instructing human vascular smooth muscle cells to generate an elastic fiber-containing extracellular matrix scaffold. J. Mol. doi: 10.1074/jbc.M107920200, Tu, Y., and Weiss, A. S. (2010). (2014). J. Biochem. Mater. 28, 379382. Single nucleotide polymorphisms and domain/splice variants modulate assembly and elastomeric properties of human elastin. doi: 10.1016/j.biomaterials.2017.01.041, Tarakanova, A., Ozsvar, J., Weiss, A. S., and Buehler, M. J. Acta Histochem. J. Biol. J. Struct. Injectable biomaterial compositions formed from tropoelastin for tissue repair and restoration. Elastin: Structure, Function, Skin Care & Supplements - Cleveland Clinic Tropoelastin, the raw material used to create 'MeTro' elastic surgical glue developed with the University of Sydney, has been found to encourage stem cell growth - with the potential to ultimately help the body repair itself. They are ubiquitous across most vertebrates other than lower vertebrates such as species from the superclass Agnatha (jawless fish) (Debelle and Tamburro, 1999). The bifunctional cross-links can undergo further condensation to form tetrafunctional desmosine or isodesmosine (Partridge, 1966). Tropoelastin promotes cell attachment and migration of several cell types including fibroblasts, endothelial cells and mesenchymal stem cells. Remodelling the extracellular matrix in development and disease. Such models could be used in conjunction with the full molecular model of tropoelastin to examine the self-assembly of discrete regions to understand the impacts of amino acid substitutions in disease. The smooth muscle cell. With the acquisition, Allergan will begin developing a new line that incorporates tropoelastin in the injectable's formula. doi: 10.1002/mabi.201800250, Tiedemann, K., Batge, B., Muller, P. K., and Reinhardt, D. P. (2001). 67-kD elastin-binding protein is a protective companion of extracellular insoluble elastin and intracellular tropoelastin. Frontiers | Tropoelastin and Elastin Assembly Combinations of these two amino acids result in domains that undergo rapid conformational sampling (Rauscher and Pomes, 2017), which, if perturbed toward a conformation that gravitate toward stability, will assemble into highly ordered amyloid-like fibrils that are not elastomeric (Rauscher et al., 2006; Roberts et al., 2015). Weiss Lab Home The spherules grow in size and are deposited onto the microfibril scaffold where they fuse into fibrillar structures (Sherratt et al., 2001). Unlike hydrophobic domains, cross-linking domains in isolation are unable to self-assemble; thus, they have been studied in the context of the cross-linking of elastin-derived biomaterials (Annabi et al., 2017; Yue et al., 2017). Together, these two properties can be tuned and exploited to give rise to an increasing number of novel biomaterials for tissue engineering and regenerative medicine, which have been recently reviewed elsewhere (Wang et al., 2020; Wen et al., 2020). eLife 6:e26526. Res. doi: 10.1016/0014-4800(65)90015-8, He, D., Chung, M., Chan, E., Alleyne, T., Ha, K. C. H., Miao, M., et al. U.S.A. 116, 20422051. 85, 593605. For Elastagen contact: Robert Daniels, CEO +61 2 9209 4054. The business could generate net sales of approximately $7 to $8 billion in 2025 from $3.8 billion in 2017. Overview of the computational and experimental methodologies that have recently contributed to our understanding of elastic fiber assembly. The importance of tropoelastins flexibility during self-assembly has also been examined in the light of natural allysine modifications, which condense to give cross-links within mature elastin (discussed further in the following section) (Ozsvar et al., 2019). Proline-poor hydrophobic domains modulate the assembly and material properties of polymeric elastin. Chem. Isolation and characterization of human elastin cDNAs, and age-associated variation in elastin gene expression in cultured skin fibroblasts. The tropoelastin that Elastagen manufactures is an identical copy of what naturally occurs in human tissue, meaning the clinical application opportunities for this has tremendous potential . (2018). 252, 351365. While tropoelastin is a flexible molecule, a combination of optical and structural analyses has defined key regions of the molecule that directly contribute to the elastomeric properties and control the cell interactions of the protein. A., Wachi, H., Davis, E. C., and Mecham, R. P. (2003). Pharm. 286, 35943610. CICADA TURNS 20: How synthetic skin biotech Elastagen changed lives Elastagen's revolutionary recombinant human tropoelastin, is identical to that present in human tissue and has many clinical applications, including effective breakthrough treatments for acne. Lab. doi: 10.1016/s0021-9258(19)43030-5, Dandurand, J., Samouillan, V., Lacabanne, C., Pepe, A., and Bochicchio, B. A cell adhesive peptide from tropoelastin promotes sequential cell attachment and spreading via distinct receptors. Healthcare Investment Banking - The Walden Group It's a stretchy protein that resembles a rubber band it can stretch out (extend) and shrink back (recoil). The hydrophobic domains contain aliphatic amino acids with proline variations that provide flexibility and the ability to assemble into higher order structures. Elastin synthesis in arterial smooth muscle cell culture. Biol. The most crucial of these properties is the ability to undergo many stretch-recoil cycles whilst maintaining the structural and functional integrity of elastic tissues over an organisms lifetime. For example, the tetrafunctional cross-link, on which the model is based, is derived from porcine elastin (Brown-Augsburger et al., 1995). 21:063001. doi: 10.1088/0965-0393/21/6/063001, Tarakanova, A., Huang, W., Weiss, A. S., Kaplan, D. L., and Buehler, M. J. 98, 416. J. Med. (2007). doi: 10.1021/bi00835a022, Lockhart-Cairns, M. P., Newandee, H., Thomson, J., Weiss, A. S., Baldock, C., and Tarakanova, A. Increased cyclic GMP levels lead to a stimulation of elastin production in ligament fibroblasts that is reversed by cyclic AMP. Proc. doi: 10.1083/jcb.68.3.411, Noda, K., Dabovic, B., Takagi, K., Inoue, T., Horiguchi, M., Hirai, M., et al. For example, the highly flexible domains 25 that were noted to generate a twisting motion in N-terminus, were positioned beside domain 6, a relatively immobile region that may assist in stabilizing the subsequent regions. doi: 10.1016/j.tibtech.2019.08.005, Wise, S. G., and Weiss, A. S. (2009). Detailed Description: No use, distribution or reproduction is permitted which does not comply with these terms. Elastin biomaterials in dermal repair. Tropoelastins amino acid sequence predominantly consists of non-polar residues including glycine, valine, alanine, and proline (Debelle and Tamburro, 1999). Pepe, A., Flamia, R., Guerra, D., Quaglino, D., Bochicchio, B., Pasquali Ronchetti, I., et al. Allergan acquired Elastagen primarily for the injectable product portfolio (acne scars/stretch marks aesthetics). 284, 22162230. The N-terminal head caps an extended coil region that consists of domains 218. Thermal compaction of disordered and elastin-like polypeptides: a temperature-dependent, sequence-specific coarse-grained simulation model. Dissection of human tropoelastin: solution structure, dynamics and self-assembly of the exon 5 peptide. The SAXS/SANS global shape of tropoelastin (Baldock et al., 2011) has been used to validate the full-atomistic computational model of tropoelastin through a geometric and topological comparison (Tarakanova et al., 2018). The hydrophobic domain 26 of human tropoelastin is unstructured in solution. Pathol. Homology models for domains 21-23 of human tropoelastin shed light on lysine crosslinking. Simul. (2021). Sci. Tropoelastin has 2 alternating domains: (1) hydrophilic, cross-linked, domains rich in Lys and Ala; and (2) hydrophobic domains (responsible for elasticity) rich in Val, Pro, and Gly, which often occur in repeats of VPGVG or VGGVG. Elastagen's technology is based on human tropoelastin . 38, 280291. Novel Recombinant Tropoelastin Implants Restore Skin Extracellular Furthermore, tropoelastins hydrophobic and cross-linking domains are arranged in alternating patterns throughout the majority of the molecule, giving rise to both inter- and intra-domain level repetition. Adv. 7:32. doi: 10.3389/fphar.2016.00032, Schmelzer, C. E. H., Heinz, A., Troilo, H., Lockhart-Cairns, M. P., Jowitt, T. A., Marchand, M. F., et al. Background: Elastin is an essential component of the dermis, providing skin with elasticity and integrity. Of most importance, the inability to acquire large quantities of pure tropoelastin historically presented a significant obstacle to experimentally characterizing its structure. Fluor: Q4 Earnings Snapshot. doi: 10.1021/bi00835a021, Gray, W. R., Sandberg, L. B., and Foster, J. U.S.A. 115, 73387343. Biochemistry 8, 28332837. doi: 10.1074/jbc.M308465200, Miao, M., Bruce, A. E., Bhanji, T., Davis, E. C., and Keeley, F. W. (2007). Primary structure of porcine tropoelastin. Hogan Lovells represented Elastagen Pty Ltd. on the deal. 396, 870873. KA domains were initially thought to form -helices and poly-proline II helices (PPII) due to the presence of cross-links which require a lysine arrangement that was postulated to be achieved via -helical configuration (Brown-Augsburger et al., 1995). Acta Gen. Subj. Bioeng. doi: 10.1021/acs.biomac.6b01759, Mackay, J. P., Muiznieks, L. D., Toonkool, P., and Weiss, A. S. (2005). Structure of the elastin gene and alternative splicing of elastin mRNA: implications for human disease. Banded fibers in tropoelastin coacervates at physiological temperatures. Biochemistry 36, 84138421. The ability to stretch and recoil arises from the biochemical properties of elastins monomer, tropoelastin (discussed below). For more information, visit Allergans website atwww.Allergan.com. Elastagen Pty Ltd, a clinical stage company developing medical device products based on recombinant tropoelastin, today announced that it has entered into a definitive agreement under which Allergan plc, a leading global biopharmaceutical company, has agreed to acquire Elastagen. J. Tropoelastins primary sequence is low in complexity and contains repetitive motifs. Elastin, arterial mechanics, and cardiovascular disease Synthesis and structural studies of a pentapeptide sequence of elastin. In addition, Elastagen has received significant support from Australian Federal Government grants and the NSW State Government Medical Devices Fund (MDF). (2017). On a per-share basis, the Irving, Texas-based company said it had profit of 1 cent. Coacervation is an endothermic, entropically favorable process through which tropoelastin monomers self-assemble into higher order n-mer structures. While the clinical stage tropoelastin platform provides multiple opportunities for aesthetics, scar remodelling and tissue repair, it also has the . Acad. Allergan is an industry leader in Open Science,a model of research and development, which defines our approach to identifying and developing game-changing ideas and innovation for better patient care. Proline and glycine control protein self-organization into elastomeric or amyloid fibrils. Synthesis and properties of crosslinked recombinant pro-resilin. Sci. doi: 10.1111/febs.14929, Hinderer, S., Shena, N., Ringuette, L. J., Hansmann, J., Reinhardt, D. P., Brucker, S. Y., et al. 27, 441450. Chem. Parameter, Testing, and Method. Cell Biol. Reichheld, S. E., Muiznieks, L. D., Huynh, Q., Wang, N., Ing, C., Miao, M., et al. Tropoelastin is a low complexity protein on both primary and secondary sequence levels. Unlike other companies that use paid endorsements and questionable data, NULASTIN science is proven by 3rd party clinical evaluation. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. They can be categorized as either hydrophobic or cross-linking based on their functionality and amino acid content (Figure 1). Biopolymers 103, 563573. doi: 10.1007/978-3-319-71530-8_13-1, Wen, Q., Mithieux, S. M., and Weiss, A. S. (2020). Tropoelastin: a versatile, bioactive assembly module - PubMed 3:100016. doi: 10.1016/j.mtbio.2019.100016, Tarakanova, A., Yeo, G. C., Baldock, C., Weiss, A. S., and Buehler, M. J. Partridge, S. M. (1966). 289, 14671477. doi: 10.1016/j.matbio.2008.02.006, Phinikaridou, A., Lacerda, S., Lavin, B., Andia, M. E., Smith, A., Saha, P., et al. Received: 17 December 2020; Accepted: 08 February 2021;Published: 25 February 2021. Latent TGF- binding protein 4 promotes elastic fiber assembly by interacting with fibulin-5. Domain 26 of tropoelastin plays a dominant role in association by coacervation. The Weiss Lab's research focuses on the use of human tropoelastin in tissue assembly and wound repair. Meanwhile, modifications to the full-atomistic model have revealed the mechanisms that contribute to aberrant fiber structure (Tarakanova et al., 2018) that have been hypothesized to predispose patients to diseases such as acquired cutis laxa (Hu et al., 2006). This temperature is also known as the transition temperature. J. Biomol. This process is reversible and thermodynamically controlled and does not require protein cleavage. J. Biol. We are making enrolling in text alerts easier than ever. N. Y. Acad. For Allergan, contact: Lisa Brown 1-862-261-7320, 1985 - 2023 BioSpace.com. doi: 10.1126/scitranslmed.aai7466, PubMed Abstract | CrossRef Full Text | Google Scholar, Avbelj, F. (2000). Cross-linking domains are capable of modulating self-assembly when incorporated into peptides and biomaterials derived from tropoelastins hydrophobic domains. Differential scanning calorimetry studies of the inverse temperature transition of the polypentapeptide of elastin and its analogues. Chem. Bochicchio, B., Yeo, G. C., Lee, P., Emul, D., Pepe, A., Laezza, A., et al. Rep. 8, 116. Elastic fiber formation: a dynamic view of extracellular matrix assembly using timer reporters. Assembly proceeds from a nucleation event and undergoes elongation in a step-wise manner to form a multimer which can occur in a head-to-tail fashion (Wise et al., 2014). 167, 94103. Integrin alpha v beta 3 binds a unique non-RGD site near the C-terminus of human tropoelastin. Elastagen is an exciting clinical-stage company with an advanced tissue repair platform based on tropoelastin. doi: 10.1073/pnas.1111615108, Yeo, G. C., Baldock, C., Wise, S. G., and Weiss, A. S. (2017). J. Biochem. Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly. Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA. Founder, Elastagen Pty Ltd (sold to Allergan/AbbVie . Sci. Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide side chains. The alignment of these three domains indicates that at least two tropoelastin molecules are required to form this tetrafunctional cross-link, thus, giving rise to the head-to-tail model of assembly involving the growth of a linear chain that can assemble laterally to form sheets and eventually form spherules (Baldock et al., 2011). Acad. Elastic fibers are present in the extracellular matrix (ECM) of vertebrate tissues, such as the skin, lungs, cardiovascular system, cartilage, and tendons. Elastic fibers are eventually formed after extensive cross-linking through a process termed maturation (Yeo et al., 2016). J. Biol. Free energy determinants of secondary structure formation: I. alpha-Helices. Lysinonorleucine. doi: 10.1161/circimaging.117.007303, Prhashanna, A., Taylor, P. A., Qin, J., Kiick, K. L., and Jayaraman, A. Developing elastic tissue. (2007). Exp. 10, 15321541. Biophys. Biol. Sci. Cooperativity between the hydrophobic and cross-linking domains of elastin. Biophys. [Epub ahead of print]. The narrow specificity to v3 and 53 may also be beneficial compared with other ECM adhesion molecules such as fibronectin (which can adhere to up to 20 types of integrin) which may compete with and modulate binding to tropoelastin, and deliver opposing effects on cell proliferation. Tropoelastin undergoes minimal energy loss during extension, similar to other polymers such as rubber and resilin (Elvin et al., 2005; Cordier et al., 2008; Baldock et al., 2011). (1983). Attempts to characterize tropoelastins structure have seen a gradual shift from the belief that tropoelastins domains have fixed structures, to understanding that the majority of its domains are capable of transitioning between random coils and transient ordered structures. 250, 9298. Tropoelastin: a versatile, bioactive assembly module. Chem. J. Biol. 282, 1248412491. The stiffness that arose due to amino acid substitutions partially determined resultant secondary structure which, in turn, impacted assembly (Prhashanna et al., 2019). 264, 88878891. doi: 10.1016/s1357-2725(98)00098-3, Duca, L., Blanchevoye, C., Cantarelli, B., Ghoneim, C., Dedieu, S., Delacoux, F., et al. Biophys. The amino acid sequence of domain 36 is unique; furthermore, its sequence confers a positively charged C-terminus comprising lysines between positively charged arginines, forming a RKRK sequence (Vrhovski et al., 1997). Cell Biol. The self-assembly properties and nanostructure of these extra teleost isoforms are yet to be investigated. Molecular dynamics modeling of aggregating tropoelastin-derived peptide chains points to the maintenance of a hydrated, disordered, liquid-like state due to the formation of short-lived inter-chain bonds (Rauscher and Pomes, 2017; Reichheld et al., 2020), mostly likely due to the inducement of random coils by PG repeats (vide supra). Coacervation of tropoelastin. Chem. Although alanine tracts within other proteins are predisposed to -helix formation (Yang and Honig, 1995; Avbelj, 2000), high helical content within tropoelastins KA domains was primarily demonstrated to persist in solvents that stabilize secondary structure, such as trifluoroethanol, rather than aqueous solution (Luo and Baldwin, 1997; Tamburro et al., 2006). Bonnans, C., Chou, J., and Werb, Z. Elastin synthesis during perinatal lung development in the rat. (2020). Transient tropoelastin nanoparticles are early-stage intermediates in the coacervation of human tropoelastin whose aggregation is facilitated by heparan sulfate and heparin decasaccharides. 9:643110. doi: 10.3389/fbioe.2021.643110. Invest. The ERC binds elastin derived peptides, which are the product of proteolytic activity of soluble and insoluble elastin by various elastases. Foster, J. J. Clin. Bioeng. Natl. Specific instructions are found in the Directions for Use. Interestingly, the location and orientation of different domains that contacted each other during self-assembly was noted to be heterogeneous, resulting in head-to-head, tail-to-tail, head-to-tail, and lateral interactions (Tarakanova et al., 2019a). Int. J. doi: 10.1111/iep.12224, Kentsis, A., and Sosnick, T. R. (1998). (2019a). doi: 10.1016/s0021-9258(19)83613-x, Miao, M., Bellingham, C. M., Stahl, R. J., Sitarz, E. E., Lane, C. J., and Keeley, F. W. (2003). The hydrophobic domains contain repetitions and variations of Val-Pro-Gly-Val-Gly motifs (Figure 1), resulting in the aforementioned low complexity of sequence (Foster et al., 1973; Gray et al., 1973). Med. Furthermore, the SAXS/SANS structure has been mapped to an elastic network model with tunable stiffness to probe the role of tropoelastins flexibility in fiber assembly (Yeo et al., 2016). Dyn. 25, 10231029. Poly (Val-Gly-Gly-Leu-Gly). doi: 10.1016/j.jsb.2004.11.005, Muiznieks, L. D., Jensen, S. A., and Weiss, A. S. (2003). Variations in the relative abundance of alternatively spliced ELN mRNA transcripts have been observed between tissues, and this diversity is thought to be necessary for the fine tuning of the mechanical characteristics of tissues to suit their unique functional requirements (Reichheld et al., 2019). doi: 10.1074/jbc.M212715200, Kumashiro, K. K., Ho, J. P., Niemczura, W. P., and Keeley, F. W. (2006). doi: 10.1016/j.matbio.2006.09.011, Miao, M., Reichheld, S. E., Muiznieks, L. D., Huang, Y., and Keeley, F. W. (2013). The alignment of the tropoelastin aggregates . Acta Biomater. Elastogenesis in human aorta: an electron microscopic study. Differential expression of two tropoelastin genes in zebrafish. Mater. (2016). Tropoelastins domains each arise from single exons of the ELN gene. 82, 335340. doi: 10.1016/j.matbio.2009.10.003, Tu, Y., Wise, S. G., and Weiss, A. S. (2010). Domain 36 of tropoelastin in elastic fiber formation. Modeling utilizing tropoelastin derivatives has demonstrated that structural compaction into both coils and globules occurs above the transition temperature of self-assembly, which may assist in explaining the anisotropic nature of mature elastin (Baul et al., 2020). A model two-component system for studying the architecture of elastin assembly in vitro. U.S.A. 84, 56805684. "We believe it's in the best strategic interest of the company to make this move, which supports Caterpillar's strategy for profitable . Subtle balance of tropoelastin molecular shape and flexibility regulates dynamics and hierarchical assembly. Res. PLoS One 7:e46130. A. Biochemistry 45, 95189530. Institute of Polymers, Composites and Biomaterials, National Research Council (IPCB-CNR), Italy, Washington University in St. Louis, United States. Evidence for the presence of alpha-aminoadipic acid delta-semialdehyde and its aldol condensation product. doi: 10.1074/jbc.M507309200, Brown-Augsburger, P., Tisdale, C., Broekelmann, T., Sloan, C., and Mecham, R. P. (1995). 28, 432441. doi: 10.1007/978-1-4684-9093-0_25, Scandolera, A., Odoul, L., Salesse, S., Guillot, A., Blaise, S., Kawecki, C., et al. Sci. Allergan plc (NYSE: AGN), headquartered in Dublin, Ireland, is a bold, global biopharmaceutical company. 84, 6880. Biomaterials 127, 4960. Baul, U., Bley, M., and Dzubiella, J. Biochemistry 8, 28372845. We are very interested in the blend of biochemistry and cell biology, as well as the tissue engineering and regenerative medicine opportunities provided by this amazing elastic protein. Cell Physiol. doi: 10.1002/bip.22663, Murata, K., and Wolf, M. (2018). Identification of an elastin cross-linking domain that joins three peptide chains. Elastin is a critical skin protein consisting of crosslinked tropoelastin. Instead, tropoelastin domains 1418 and 36 (RKRK sequence) have been found to bind to both integrins. 278, 1849118498. J. Biol. I thank the Elastagen team for their hard work and dedication in developing our innovative tropoelastin product pipeline and look forward to working with Allergan to take these products to market., Commenting on the transaction, Elastagens founding scientist Prof Anthony Weiss added:Our technology has come a long way from the lab bench at the University of Sydney towards developing products for patients around the world. Biol. Similar to other ECM proteins, such as collagen, tropoelastin covalently cross-links via its lysines. doi: 10.1128/mcb.26.5.1700-1709.2006, Mecham, R. P. (1991). 120, 419426. doi: 10.1006/excr.1995.1321, Hinek, A., and Rabinovitch, M. (1994). J. Biol. Stem cell growth accelerated by tropoelastin protein Proc. 266, 308314. Matrix Biol. Molecular model for elastin structure and function. Elastases can be in the form of serine- (e.g., Ela-2), cysteine- (e.g., cathepsin I), or matrix metalloproteinases (MMP-2, -7, -9, and -12), and bioactive peptides include the VGVAPG peptide. Ltd., which was sold to Allergan, now a division of AbbVie. 258, 118. Similarly, a mutation model associated with cutis laxa, or loose skin disease (Hu et al., 2006), was found to exhibit higher stability compared with the wild-type molecule due to the increased longevity of its salt bridges (Hu et al., 2006; Tarakanova et al., 2018). Sequence and structure determinants for the self-aggregation of recombinant polypeptides modeled after human elastin. doi: 10.1016/s0022-5320(83)80021-5, Broekelmann, T. J., Kozel, B. Lyophilized Powder. Acad. J. doi: 10.1038/sj.jid.5700047, Indik, Z., Yeh, H., Ornstein-Goldstein, N., Kucich, U., Abrams, W., Rosenbloom, J. C., et al. Our understanding of key aspects of the assembly process have been unclear due to the intrinsic properties of elastin and tropoelastin that render them difficult to study. Recycling of the 67-kDa elastin binding protein in arterial myocytes is imperative for secretion of tropoelastin. Characterization of the complete human elastin gene. This canonical computational structure was determined to be highly similar to the envelope found via SAXS/SANS, where both consist of an extended molecular body accompanied by a protruding foot (Baldock et al., 2011). J. More surprisingly, tropoelastins cross-linking domains are also capable of similar transitions between ordered and disordered structures. However, there are aspects of this model that warrant further investigation. Biochemistry 52, 77317741. Allergans success is powered by our global colleagues commitment to being Bold for Life. Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins. A., Rongish, B. J., Czirok, A., Zach, J., Little, C. D., Davis, E. C., et al. Molecular docking studies utilizing tropoelastin and the 3D structure of LOX1 (Vallet et al., 2018) may assist in our understanding as to whether the enzyme has a preference for modifying particular tropoelastin residues. Collapse Section. III. Biol. doi: 10.1073/pnas.1801205115, Tarakanova, A., Yeo, G. C., Baldock, C., Weiss, A. S., and Buehler, M. J. Rush to Beauty Anticipates New Line of Dermal Fillers from Allergan The conserved C-terminus is an area of the molecule of particular biological importance in that it is required for both incorporation into elastin and for cellular interactions. Production of recombinant human tropoelastin: Characterization and 276, 3603536042. Matrix Biol. Tropoelastin cannot readily be prepared in quantity from natural sources and this has limited research in several important areas including structure/function relationships and fiber assembly.