Conformational Properties of Helical Protein Polymers with Varying Densities of Chemically Reactive Groups

Farmer, Robin S.; Argust, Lindsey M.; Sharp, Jared D.; Kiick, Kristi L.

doi:10.1021/ma051534t

Cited by 28 publications

(68 citation statements)

References 63 publications

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“…In the alanine-rich polypeptides described here, glutamine has been employed for improved solubility, while glutamic acid has been included for subsequent chemical modification. The thermal and conformational behaviors of these longer repetitive alanine-rich polypeptides in solution at low pH generally follow trends predicted by the study of shorter alanine-rich sequences (15,16). In addition, the modification of the glutamic acid residues with amine-functionalized monosaccharides does not significantly affect the conformational behavior of the polypeptides, and specific helical glycopolypeptides have shown promise as toxin inhibitors (30).…”

Section: Introductionsupporting

confidence: 53%

“…Protocols for construction of DNA plasmids and expression of 17-H-3 and 35-H-6 have been reported previously (15); these protocols were employed in the synthesis of 17-H-6. Briefly, the DNA sequence encoding the amino acid sequence, [AAAQEAAAAQAAAQAEAAQAAQ], was ligated into a modified expression plasmid, pET28b-JS1 (15).…”

Section: Gene Construction and Polypeptide Expressionmentioning

confidence: 99%

“…These strategies have been employed in the production of natural protein mimics including silk (1)(2)(3)(4)(5), elastin (6)(7)(8)(9)(10)(11)(12), and collagen (13,14), which, although having great potential in materials-based applications, can be difficult to obtain in large quantities from their natural sources. Artificial proteins have also been designed to take advantage of the absolute control over amino acid sequence and molecular weight and the secondary structural preferences of specific amino acids and amino acid consensus sequences (15)(16)(17)(18)(19)(20)(21). Accordingly, the versatility of these synthetic methods has permitted the production of a variety of protein polymers with well-defined secondary structures designed for a specific function or application.…”

Section: Introductionmentioning

confidence: 99%

“…Accordingly, the versatility of these synthetic methods has permitted the production of a variety of protein polymers with well-defined secondary structures designed for a specific function or application. Numerous studies have focused on the synthesis of repetitive amino acid sequences that adopt β-sheet, coiledcoil or random coil structures (17,19,20,(22)(23)(24)(25)(26)(27)(28)(29), although there have been fewer reports about sequences designed to adopt monomeric α-helical secondary structures (15,16,18,30).…”

Section: Introductionmentioning

confidence: 99%

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Evaluation of Conformation and Association Behavior of Multivalent Alanine-Rich Polypeptides

et al. 2007

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Purpose-Helical alanine-rich polypeptides with functional groups displayed along the backbone can display desired molecules such as saccharides or therapeutic molecules at a prescribed spacing. Because these polypeptides have promise for application as biomaterials, the conformation and association of these molecules have been investigated under biologically relevant conditions. Methods-Three polypeptide sequences, 17-H-3, 17-H-6, and 35-H-6, have been produced through recombinant techniques. Circular dichroic (CD) spectroscopy was used to monitor the secondary structure of the polypeptides in PBS (phosphate buffered saline, pH 7.4). The aggregation behavior in PBS was monitored via analytical ultracentrifugation and non-denaturing polyacrylamide gel electrophoresis.Results-The three polypeptides adopt a highly helical structure at low and ambient temperatures, and when heated, undergo a helix-to-coil transition, typical of other alanine-rich peptide sequences. The melting temperatures and van't Hoff enthalpies, extracted from the CD data, suggest similar stability of the sequences. Although alanine-rich sequences can be prone to aggregation, there is no indication of aggregation for the three polypeptides at a range of concentrations relevant for possible biological applications.Conclusions-The helical polypeptides are monomeric under biologically relevant conditions enabling application of these polypeptides as useful scaffolds for ligand or drug display.

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Section: Introductionsupporting

confidence: 53%

Section: Gene Construction and Polypeptide Expressionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Evaluation of Conformation and Association Behavior of Multivalent Alanine-Rich Polypeptides

et al. 2007

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“…[44,45 ] The assembled nanostructure of 17H6 is strongly dependent on its microenvironment, and can be controlled by changes in the initial solution conditions, in which the assembly is conducted, particularly pH and temperature. At neutral pH, the polypeptide adopts a helical, non-aggregated structure.…”

mentioning

confidence: 99%

One‐Dimensional Gold Nanoparticle Arrays by Electrostatically Directed Organization Using Polypeptide Self‐Assembly

et al. 2009

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The study of interactions between particles organized in a linear configuration is interesting from a quantum mechanical perspective, and the anisotropic properties of linear assemblies is of potential interest for the development of solid-state devices. [1][2][3] This anisotropy may be manifested as a difference in the magnetization and coercivity obtained in a magneticnanoparticle array when a field is applied along the chain or orthogonal to it. [4,5 ] Nonlinear electrical characteristics [3] or dichroism in the optical spectra with longitudinal and transverse polarizations of light [6,7 ] in metal nanoparticle arrays are other examples of such anisotropy, and the construction of such arrays would offer opportunities in multiple applications. Engineering matter at submicron length scales has been an area largely dominated by top-down methodologies. Control of interparticle spacing in metal-nanoparticle arrays by using techniques such as electron beam lithography has been found to have a dramatic impact on the optical response of the nanoparticle assembly, [8][9][10] ] and has implications in fields such as plasmonics [11] and energy transport. [12,13 ] The use of templates such as carbon nanotubes [14] and linear pores[15] to construct one-dimensional nanostructures has been demonstrated previously. In addition, polymers have recently begun to play an increasingly active role as elements that can reproducibly direct the arrangement of nanoparticles into functional geometries. [16,17 ] Self assembling systems offer convenient yet powerful bottom-up strategies for the creation of nanostructures that can be deployed in the realization of functional nanoscale devices. [18,19 ] The utilization of biomolecules such as DNA, [3, 20 -24 ] and protein-based materials [25][26][27] or viruses [28,29 ] to dictate the organization of nanoparticles has been shown to be an effective and robust paradigm. The use of peptide-based structures [30,31 ] in nanotechnology confers numerous advantages such as the specification of assembled nanostructure by changes in the primary sequence of the peptide, as well as the adoption of various hierarchical morphologies **

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Biosynthesis of Protein‐Based Polymeric Materials

Farmer¹,

Charati²,

Kiick³

2007

Macromolecular Engineering

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Conformational Properties of Helical Protein Polymers with Varying Densities of Chemically Reactive Groups

Cited by 28 publications

References 63 publications

Evaluation of Conformation and Association Behavior of Multivalent Alanine-Rich Polypeptides

Evaluation of Conformation and Association Behavior of Multivalent Alanine-Rich Polypeptides

One‐Dimensional Gold Nanoparticle Arrays by Electrostatically Directed Organization Using Polypeptide Self‐Assembly

Biosynthesis of Protein‐Based Polymeric Materials

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