Electrochemical characterization of the stimuli-response of surface-immobilized elastin-like polymers

Morales, M. Ángeles F.; Paiva, Wynter; Marvin, Laura; Balog, Eva Rose M.; Halpern, Jeffrey Mark

doi:10.1039/c9sm01681c

Cited by 14 publications

(12 citation statements)

References 41 publications

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“…Surface-grafted elastin has found many applications including in switchable interfaces 17 – 19 , vascular engineering 20 , 21 , and controlling electrode architecture 22 , 23 . Surface-grafting of elastin-like polypeptides has been facilitated by amine-reactive crosslinker chemistry with N-hydroxysuccinimide 24 , thiol binding to gold 25 – 27 , affinity sequences 28 , 29 , and physical adsorption 30 , 31 . All the listed methods involve incubation of elastin-like polypeptide molecules near the surface of interest, leaving the interaction between elastin-like polypeptides and the surfaces uncontrolled and the subsequent properties often unpredictable.…”

Section: Introductionmentioning

confidence: 99%

Grafting of short elastin-like peptides using an electric field

Pramounmat

Asaei

Hostert

et al. 2022

Sci Rep

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Surface-grafted elastin has found a wide range of uses such as sensing, tissue engineering and capture/release applications because of its ability to undergo stimuli-responsive phase transition. While various methods exist to control surface grafting in general, it is still difficult to control orientation as attachment occurs. This study investigates using an electric field as a new approach to control the surface-grafting of short elastin-like polypeptide (ELP). Characterization of ELP grafting to gold via quartz crystal microbalance with dissipation, atomic force microscopy and temperature ramping experiments revealed that the charge/hydrophobicity of the peptides, rearrangement kinetics and an applied electric field impacted the grafted morphology of ELP. Specifically, an ELP with a negative charge on the opposite end of the surface-binding moiety assembled in a more upright orientation, and a sufficient electric field pushed the charge away from the surface compared to when the same peptide was assembled in no electric field. In addition, this study demonstrated that assembling charged ELP in an applied electric field impacts transition behavior. Overall, this study reveals new strategies for achieving desirable and predictable surface properties of surface-bound ELP.

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Section: Introductionmentioning

confidence: 99%

Grafting of short elastin-like peptides using an electric field

Pramounmat

Asaei

Hostert

et al. 2022

Sci Rep

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“…As a solution, elastin has been combined with gelatin and carbon nanotubes to create stronger matrices . By changing the molecular design of ELPs, their hydrophobicity can be tuned to modify their transition temperatures and sensitize them to environmental factors like pH and ionic strength . Cysteine residues in ELPs are particularly useful to bind with gold electrodes in an impedimetric salt and humidity sensor reported …”

Section: Proteins As Scaffoldsmentioning

confidence: 99%

“…206 By changing the molecular design of ELPs, their hydrophobicity can be tuned to modify their transition temperatures and sensitize them to environmental factors like pH and ionic strength. 207 Cysteine residues in ELPs are particularly useful to bind with gold electrodes in an impedimetric salt and humidity sensor reported. 207 Elastin has also been coexpressed with silk in bacterial systems by varying the number of the elastin and silk blocks and including periodic cysteine residues in the elastin blocks to produce biomaterials that inherently combine the favorable properties of the two.…”

Section: Collagenmentioning

confidence: 99%

“…207 Cysteine residues in ELPs are particularly useful to bind with gold electrodes in an impedimetric salt and humidity sensor reported. 207 Elastin has also been coexpressed with silk in bacterial systems by varying the number of the elastin and silk blocks and including periodic cysteine residues in the elastin blocks to produce biomaterials that inherently combine the favorable properties of the two. Disulfide cross-linking of elastin−silk composite fibers results in the formation of cytocompatible and hydrophilic membranes.…”

Section: Collagenmentioning

confidence: 99%

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The Evolving Role of Proteins in Wearable Sweat Biosensors

Saldanha

Cai

Courchesne

2021

ACS Biomater. Sci. Eng.

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Sweat is an increasingly popular biological medium for fitness monitoring and clinical diagnostics. It contains an abundance of biological information and is available continuously and noninvasively. Sweat-sensing devices often employ proteins in various capacities to create skin-friendly matrices that accurately extract valuable and time-sensitive information from sweat. Proteins were first used in sensors as biorecognition elements in the form of enzymes and antibodies, which are now being tuned to operate at ranges relevant for sweat. In addition, a range of structural proteins, sometimes assembled in conjunction with polymers, can provide flexible and compatible matrices for skin sensors. Other proteins also naturally possess a range of functionalitiesas adhesives, charge conductors, fluorescence emitters, and power generatorsthat can make them useful components in wearable devices. Here, we examine the four main components of wearable sweat sensorsthe biorecognition element, the transducer, the scaffold, and the adhesive and the roles that proteins have played so far, or promise to play in the future, in each component. On a case-by-case basis, we analyze the performance characteristics of existing protein-based devices, their applicable ranges of detection, their transduction mechanism and their mechanical properties. Thereby, we review and compare proteins that can readily be used in sweat sensors and others that will require further efforts to overcome design, stability or scalability challenges. Incorporating proteins in one or multiple components of sweat sensors could lead to the development and deployment of tunable, greener, and safer biosourced devices.

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“…Graphene nanofibers, through careful adjustments in their structure, can be superior in biosensing to carbon nanotubes (CNTs) [27][28][29][30] as well as less expensive in general [5,6] due to high adsorption from their adjustable porosity and surface area. Nanofibers formed from long peptide chains, such as elastin-like polypeptides and elastin-like peptide amphiphiles, have also been explored for their stimuli responsive and adsorptive behavior [31][32][33][34]. In short, the physical properties of nanofibers demonstrate high favorability in sensor applications over traditional nanomaterials.…”

Section: Introductionmentioning

confidence: 99%

Perspective on Nanofiber Electrochemical Sensors: Design of Relative Selectivity Experiments

2021

Self Cite

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The use of nanofibers creates the ability for non-enzymatic sensing in various applications and greatly improves the sensitivity, speed, and accuracy of electrochemical sensors for a wide variety of analytes. The high surface area to volume ratio of the fibers as well as their high porosity, even when compared to other common nanostructures, allows for enhanced electrocatalytic, adsorptive, and analyte-specific recognition mechanisms. Nanofibers have the potential to rival and replace materials used in electrochemical sensing. As more types of nanofibers are developed and tested for new applications, more consistent and refined selectivity experiments are needed. We applied this idea in a review of interferant control experiments and real sample analyses. The goal of this review is to provide guidelines for acceptable nanofiber sensor selectivity experiments with considerations for electrocatalytic, adsorptive, and analyte-specific recognition mechanisms. The intended presented review and guidelines will be of particular use to junior researchers designing their first control experiments, but could be used as a reference for anyone designing selectivity experiments for non-enzymatic sensors including nanofibers. We indicate the importance of testing both interferants in complex media and mechanistic interferants in the selectivity analysis of newly developed nanofiber sensor surfaces.

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Electrochemical characterization of the stimuli-response of surface-immobilized elastin-like polymers

Abstract: The stimuli-responsive behavior of surface-immobilized ELPs, corresponding to proposed extended and collapsed states, was characterized using electrochemical impedance spectroscopy.

Cited by 14 publications

References 41 publications

Grafting of short elastin-like peptides using an electric field

Grafting of short elastin-like peptides using an electric field

The Evolving Role of Proteins in Wearable Sweat Biosensors

Perspective on Nanofiber Electrochemical Sensors: Design of Relative Selectivity Experiments

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