A pH-responsive interface derived from resilin-mimetic protein Rec1-resilin

Truong, My Y.; Dutta, Naba K.; Choudhury, Namita Roy; Kim, Misook; Elvin, Christopher M.; Hill, Anita J.; Thierry, Benjamin; Vasilev, Krasimir

doi:10.1016/j.biomaterials.2010.02.019

Cited by 54 publications

(64 citation statements)

References 51 publications

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“…These effects collectively produce a threefold variation in brush thickness over this pH range. Such pH-responsive thickness changes were recently reported in a more modest form (1.2-1.6-fold) for immobilized resilin-mimetic protein bilayers 34 . When the magnitude of the charge on the protein at various pH values (Fig.…”

Section: Resultssupporting

confidence: 59%

Stimuli-sensitive intrinsically disordered protein brushes

et al. 2014

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Grafting polymers onto surfaces at high density to yield polymer brush coatings is a widely employed strategy to reduce biofouling and interfacial friction. These brushes almost universally feature synthetic polymers, which are often heterogeneous and do not readily allow incorporation of chemical functionalities at precise sites along the constituent chains. To complement these synthetic systems, we introduce a biomimetic, recombinant intrinsically disordered protein that can assemble into an environment-sensitive brush. This macromolecule adopts an extended conformation and can be grafted to solid supports to form oriented protein brushes that swell and collapse dramatically with changes in solution pH and ionic strength. We illustrate the value of sequence specificity by using proteases with mutually orthogonal recognition sites to modulate brush height in situ to predictable values. This study demonstrates that stimuli-responsive brushes can be fabricated from proteins and introduces them as a new class of smart biomaterial building blocks.

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Section: Resultssupporting

confidence: 59%

Stimuli-sensitive intrinsically disordered protein brushes

et al. 2014

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“…[11] PAMAM dendrimers have been shown to be capable of carrying and releasing two types of drugs in a controlled manner. [12] Therefore, stimuliresponsive dendrimers offer a unique platform for many applications, [6,13] particularly biomedical engineering in developing intelligent devices that are able to sense biosignals or microenvironments, [14] such as tumor-sensitive contrast agents, [9,15] tumor-targeted drug release carriers, [16,17] and gene delivery carriers. [18] Dual responses to both temperature and pH offer two parameters for manipulating nanocarriers so as to achieve better targeting and efficacy in complicated microenvironments [19] or for other functions such as triggered release.…”

Section: Introductionmentioning

confidence: 99%

Degradable Dual pH‐ and Temperature‐Responsive Photoluminescent Dendrimers

Shen

Zhang

et al. 2011

Chemistry A European J

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Poly(β-aminoester) dendrimers have been prepared. These systems represent the first degradable dual pH- and temperature-responsive dendrimers displaying photoluminescence. The pH/temperature sensitivities are interrelated; the lower critical solution temperature of the dendrimer decreases as the pH of the solution is increased. The sensitivities are mainly due to phase changes of the surface groups with changes in pH or temperature. These dual-responsive dendrimers are very useful in drug delivery. They may be loaded with a hydrophobic drug at low temperature without using organic solvents. The loaded drug is released very slowly and steadily at 37 °C and physiological pH, but can be quickly released at acidic pH, for example the lysosomal pH (pH 4-5), for intracellular drug release. These dendrimers also display strong photoluminescence, which can be exploited for monitoring drug loading and release. Thus, poly(β-aminoester) dendrimers constitute ideal drug carriers since their thermal sensitivity allows the loading of drugs without using organic solvents, their pH sensitivity permits fast intracellular drug release, and their photoluminescence provides a means of monitoring drug loading and release.

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“…Another study exploited the architecture found in spider silk 20 proteins to engineer materials with remarkable extensibility and strength 29 ( Figure 2B). The use of proteins in the rational design of biomimetic materials and functional biomaterials for tissue engineering, lubrication and medicine, is now a field of considerable and growing current interest 23,28,38 . To exploit 25 proteins for the design of artificial, novel materials or to utilise them in nanomechanical systems as springs, switches or sensors 23 , it will be necessary to have a tool-box of proteins available with known or predictable mechanical properties.…”

Section: Introductionmentioning

confidence: 99%

Towards design principles for determining the mechanical stability of proteins

Hoffmann

Tych

Hughes

et al. 2013

Phys. Chem. Chem. Phys.

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The successful integration of proteins into bionanomaterials with specific and desired function requires an accurate understanding of their material properties. Two such important properties are their mechanical stability and malleability. While single molecule manipulation techniques 15 now routinely provide access to these, there is a need to move towards predictive tools that can rationally identify proteins with desired material properties. We provide a comprehensive review of the available experimental data on the single molecule characterisation of proteins using the 20 atomic force microscope. We uncover a number of empirical relationships between the measured mechanical stability of a protein and its malleability which provide a set of simple tools which might be employed to estimate properties of previously uncharacterised proteins. 25

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A pH-responsive interface derived from resilin-mimetic protein Rec1-resilin

Cited by 54 publications

References 51 publications

Stimuli-sensitive intrinsically disordered protein brushes

Stimuli-sensitive intrinsically disordered protein brushes

Degradable Dual pH‐ and Temperature‐Responsive Photoluminescent Dendrimers

Towards design principles for determining the mechanical stability of proteins

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