Circular dichroism studies on repeating polypeptide sequences of abductin

Bochicchio, Brigida; Pepe, Antonietta; Tamburro, Antonio Mario

doi:10.1002/chir.20172

Cited by 15 publications

(19 citation statements)

References 37 publications

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“…Based on our knowledge of the relationship of phase behavior and disorder in ELPs, it is a reasonable hypothesis that other intrinsically disordered proteins may also be capable of similar phase behavior. In fact, this property has already been noted for several mechanically active, elastomeric domains, including resilin and abductin, which are capable of UCST, LCST, or a combination of the two behaviors[36,88,92]. When considering the design of combinatorial materials with ELPs, an obvious first step is the inclusion of similar elastomeric domains in either mixtures or encoded together at the sequence level.…”

Section: Discussionmentioning

confidence: 87%

“…An interesting observation requiring further investigation is the close sequence relationship between lamprin and ELP, though lamprin, unlike ELPs, can adopt a β‐sheet conformation in aqueous solution. Their biophysical similarity is noteworthy given the disparity in their primary sequence and composition, especially between elastin and resilin/HMW gluten[88]. This leads us to the questions, “What is the cause for this similarity?” and “How we may better attribute their differences in sequence to differences in solution properties?” Although each unit (besides lamprin) is disordered, they seem to have used different combinations of amino acids to achieve disorder.…”

Section: Other Elastomeric Polymers With Idp Characteristicsmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 87%

Section: Other Elastomeric Polymers With Idp Characteristicsmentioning

confidence: 99%

Elastin‐like polypeptides as models of intrinsically disordered proteins

2015

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“…53 The CD spectrum of AB12 in TFE ( Figure 3B) shows a strong positive peak at 195 nm and a small negative band at ∼225 nm, which indicates a dominant conformation of type II β-turns together with a small contribution of unordered structures. 33,61 The dominant PPII helix structure of AB12 in aqueous solution was also observed with other short synthetic abductinlike peptides, such as GGMGGG, GMGGG, FGGMGGG, and FGGMGGGNAG. 33 GMGGG and GGMGGG also exhibit type II β-turns in TFE.…”

Section: ■ Materials and Methodsmentioning

confidence: 72%

“…33,61 The dominant PPII helix structure of AB12 in aqueous solution was also observed with other short synthetic abductinlike peptides, such as GGMGGG, GMGGG, FGGMGGG, and FGGMGGGNAG. 33 GMGGG and GGMGGG also exhibit type II β-turns in TFE. 33,34 The coexistence of PPII and unordered structures of AB12 in water is similar to what was seen with longer synthetic abductin-like peptides (AGGMGGGNAGAGGMGGGMAGAGGMG).…”

Section: ■ Materials and Methodsmentioning

confidence: 72%

“…Most synthetic abductin-based peptides adopt polyproline II (PPII) structures, which are left-handed helices, in aqueous solution, whereas they have type II β-turns in trifluoroethanol (TFE), which is a more hydrophobic solvent. 33 Coexistence of PPII and type II β-turns and temperature-induced multiconformational transitions were observed with longer synthetic abductinlike peptides such as (FGGMGGGNAG) 4 in hexafluoroisopropanol (HFIP). 34 To our knowledge, this work is the first study to describe the synthesis and expression of recombinant abductin-based proteins.…”

Section: ■ Introductionmentioning

confidence: 98%

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Synthesis and Characterization of Recombinant Abductin-Based Proteins

Renner

Liu

2013

Biomacromolecules

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Recombinant proteins are promising tools for tissue engineering and drug delivery applications. Protein-based biomaterials have several advantages over natural and synthetic polymers, including precise control over amino acid composition and molecular weight, modular swapping of functional domains, and tunable mechanical and physical properties. In this work, we describe recombinant proteins based on abductin, an elastomeric protein that is found in the inner hinge of bivalves and functions as a coil spring to keep shells open. We illustrate, for the first time, the design, cloning, expression, and purification of a recombinant protein based on consensus abductin sequences derived from Argopecten irradians . The molecular weight of the protein was confirmed by mass spectrometry, and the protein was 94% pure. Circular dichroism studies showed that the dominant structures of abductin-based proteins were polyproline II helix structures in aqueous solution and type II β-turns in trifluoroethanol. Dynamic light scattering studies illustrated that the abductin-based proteins exhibit reversible upper critical solution temperature behavior and irreversible aggregation behavior at high temperatures. A LIVE/DEAD assay revealed that human umbilical vein endothelial cells had a viability of 98 ± 4% after being cultured for two days on the abductin-based protein. Initial cell spreading on the abductin-based protein was similar to that on bovine serum albumin. These studies thus demonstrate the potential of abductin-based proteins in tissue engineering and drug delivery applications due to the cytocompatibility and its response to temperature.

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β‐Sheet Breaker Peptides Containing α,β‐Dehydrophenylalanine: Synthesis and In Vitro Activity Studies

et al. 2014

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The synthesis and fibrillogenesis‐inhibiting activity of the new peptide derivatives 1–6, containing α,β‐unsaturated phenylalanines, are reported. These compounds are related to the pentapeptide Ac‐LPFFD‐NH2 (iAβ5p), which was designed by Soto and co‐workers and is commonly accepted as a lead compound for fibrillogenesis inhibition . Their activities are determined by Thioflavin T binding assay, far‐UV circular dichroism (CD) spectroscopy , and SEM; in addition, their structures in solution are studied through far‐UV CD and FTIR spectroscopy. The presence of two α,β‐unsaturated phenylalanines increases the fibrillogenesis inhibiting activity significantly in comparison with the lead compound. The interactions between the Aβ1–40 and the inhibitors using electrospray ionization mass spectrometry are also studied. The analyses prove the presence of noncovalent complexes of Aβ1–40 with iAβ5p and its derivatives 1–3 with stoichiometries of 1:1 and 2:1, and the results are independent of time and Aβ1–40/inhibitor ratio.

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Circular dichroism studies on repeating polypeptide sequences of abductin

Cited by 15 publications

References 37 publications

Elastin‐like polypeptides as models of intrinsically disordered proteins

Elastin‐like polypeptides as models of intrinsically disordered proteins

Synthesis and Characterization of Recombinant Abductin-Based Proteins

β‐Sheet Breaker Peptides Containing α,β‐Dehydrophenylalanine: Synthesis and In Vitro Activity Studies

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