Design and application of stimulus-responsive peptide systems

Chockalingam, Karuppiah; Blenner, Mark; Banta, Scott

doi:10.1093/protein/gzm008

Cited by 92 publications

(73 citation statements)

References 90 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…[4][5][6][7] The ability to control the transition between different structural states presents an opportunity for their utilization in applications such as protein purification, biosensors, development of ''smart'' therapeutics, and other bionanotechnologies. 8,9 For example, the elastin-like peptides undergo a change in structure on changes in temperature and have been employed in applications including protein purification and temperature-controlled binding. 10,11 The ability to switch between a disordered and an ordered structure with an intrinsic binding site may be useful in biosensor development where the ability to modulate binding is desired.…”

Section: Introductionmentioning

confidence: 99%

Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance

Shur

Banta

2011

Protein Science

Self Cite

View full text Add to dashboard Cite

Intrinsically disordered peptides (IDPs) have recently garnered much interest because of their role in biological processes such as molecular recognition and their ability to undergo stimulus-responsive conformational changes. The block V repeat-in-toxin motif of the Bordetella pertussis adenylate cyclase is an example of an IDP that undergoes a transition from a disordered state to an ordered beta roll conformation in the presence of calcium ions. In solution, a C-terminal capping domain is necessary for this transition to occur. To further explore the conformational behavior and folding requirements of this IDP, we have cysteine modified three previously characterized constructs, allowing for attachment to the gold surface of a quartz crystal microbalance (QCM). We demonstrate that, while immobilized, the C-terminally capped peptide exhibits similar calcium-binding properties to what have been observed in solution. In addition, immobilization on the solid surface appears to enable calcium-responsiveness in the uncapped peptides, in contrast to the behavior observed in solution. This work demonstrates the power of QCM as a tool to study the conformational changes of IDPs immobilized on surfaces and has implications for a range of potential applications where IDPs may be engineered and used including protein purification, biosensors, and other bionanotechnology applications.

show abstract

Section: Introductionmentioning

confidence: 99%

Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance

Shur

Banta

2011

Protein Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…And, just as function stems from structure, it is also controlled within the protein-engineering scheme of materials design. There are a number of successful examples of hydrogels designed for tissueengineering and drug-delivery applications that use functional protein domains to obtain structural responsiveness to environmental cues (2)(3)(4). These examples include responsiveness to pH (5), temperature (6), shear stress (7), and ligand binding (8,9) among others (refs.…”

mentioning

confidence: 99%

Bioelectrocatalytic hydrogels from electron-conducting metallopolypeptides coassembled with bifunctional enzymatic building blocks

Wheeldon

Gallaway

Barton

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Here, we present two bifunctional protein building blocks that coassemble to form a bioelectrocatalytic hydrogel that catalyzes the reduction of dioxygen to water. One building block, a metallopolypeptide based on a previously designed triblock polypeptide, is electron-conducting. A second building block is a chimera of artificial ␣-helical leucine zipper and random coil domains fused to a polyphenol oxidase, small laccase (SLAC). The metallopolypeptide has a helix-random-helix secondary structure and forms a hydrogel via tetrameric coiled coils. The helical and random domains are identical to those fused to the polyphenol oxidase. Electron-conducting functionality is derived from the divalent attachment of an osmium bis-bipyrdine complex to histidine residues within the peptide. Attachment of the osmium moiety is demonstrated by mass spectroscopy (MS-MALDI-TOF) and cyclic voltammetry. The structure and function of the ␣-helical domains are confirmed by circular dichroism spectroscopy and by rheological measurements. The metallopolypeptide shows the ability to make electrical contact to a solid-state electrode and to the redox centers of modified SLAC. Neat samples of the modified SLAC form hydrogels, indicating that the fused ␣-helical domain functions as a physical cross-linker. The fusion does not disrupt dimer formation, a necessity for catalytic activity. Mixtures of the two building blocks coassemble to form a continuous supramolecular hydrogel that, when polarized, generates a catalytic current in the presence of oxygen. The specific application of the system is a biofuel cell cathode, but this protein-engineering approach to advanced functional hydrogel design is general and broadly applicable to biocatalytic, biosensing, and tissue-engineering applications.biocatalysis ͉ biofuel cell ͉ biomaterial ͉ laccase ͉ protein P rotein engineering provides the tool set to design and produce peptides and proteins that form the building blocks of new bio-inspired materials. The tool set allows for the manipulation of natural and artificial DNA sequences encoding the peptides or proteins of interest, and the subsequent biological production of the translated products. The methodology is powerful in that it allows for exact control over the identity and sequence of each residue and, consequently, the structural folding patterns of the resultant peptides or proteins (1). And, just as function stems from structure, it is also controlled within the protein-engineering scheme of materials design. There are a number of successful examples of hydrogels designed for tissueengineering and drug-delivery applications that use functional protein domains to obtain structural responsiveness to environmental cues (2-4). These examples include responsiveness to pH (5), temperature (6), shear stress (7), and ligand binding (8, 9) among others (refs. 2 and 10; ref. 3 and references therein). A wider range of applications, such as bioelectrocatalysis and biosensing, will benefit from the advantages of protein-based materials design pr...

show abstract

“…Rational design (Arnold, 1993) Site-directed mutagenesis (Arnold, 1993), (Antikainen & Martin, 2005) Evolutionary methods/directed evolution (Arnold, 1993) Random mutagenesis (Antikainen & Martin, 2005), (Wong et al, 2006), (Jackson et al, 2006), (Labrou, 2010) DNA shuffling (Antikainen & Martin, 2005), (Jackson et al, 2006) Molecular dynamics (Anthonsen et al, 1994) Homology modeling (Anthonsen et al, 1994) 'MolCraft'in vitro protein evolution systems (Shiba, 2004) Computational methods (computational protein design) (Jackson et al, 2006), (Van der Sloot et al, 2009), (Golynskiy & Seelig, 2010) Receptor-based QSAR methods (Lushington et al, 2007) NMR (Anthonsen et al, 1994) X-ray crystallography (Jackson et al, 2006) Peptidomimetics (Venkatesan & Kim, 2002) Phage display technology (Antikainen & Martin, 2005), (Sidhu & Koide, 2007), (Chaput et al, 2008) Cell surface display technology (Antikainen & Martin, 2005), (Gai & Wittrup, 2007), (Chaput et al, 2008) Flow cytometry / Cell sorting (Mattanovich & Borth, 2006 ) Cell-free translation systems (Shimizu et al, 2006) Designed divergent evolution (Yoshikuni & Keasling, 2007) Stimulus-responsive peptide systems (Chockalingam et al, 2007) Mechanical engineering of elastomeric proteins (Li, 2008) Engineering extracellular matrix variants (Carson & Barker, 2009) Traceless Staudinger ligation (Tam & Raines, 2009) De novo enzyme engineering (Golynskiy & Seelig, 2010) mRNA display …”

Section: Methods Name Reference(s)mentioning

confidence: 99%

“…Directed evolution of stimulus-responsive peptides, however, requires an appropriate selection or screening scheme. Thus, protein-based conformational change sensors (CCSs) were developed using immunofluorescence and recombinant DNA technology (Chockalingam et al, 2007).…”

Section: Protein Engineering 36mentioning

confidence: 99%