Fluorescent Protein Senses and Reports Mechanical Damage in Glass‐Fiber‐Reinforced Polymer Composites

Makyła, Katarzyna; Müller, Christoph; Lörcher, Samuel; Winkler, Thomas; Nussbaumer, Martin G.; Eder, Michaela; Bruns, Nico

doi:10.1002/adma.201205226

Cited by 58 publications

(54 citation statements)

References 31 publications

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“…6). Makyła et al [73] polymer composites with eYFP as the mechanophore whose fluorescence was highly dependent on its secondary structures. In their case, mechanical perturbation of the β-barrel structure from the fiber fractures or fiber-matrix de-bonding leads to remarkable change of fluorescence (Fig.…”

Section: Mechanoluminescent Polymers With Covalent Mechanophoresmentioning

confidence: 99%

Recent advances in mechanoluminescent polymers

Yuan

Chen

2016

Sci. China Mater.

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In recent years, mechanoluminescence from polymers is emerging as a new cutting-edge area of polymer mechanochemistry research. It refers to the release of energy from polymers in the form of light when they are under various mechanical stimuli. To spur more researchers to join in such interesting and new burgeoning area, and promote its development to practical applications, in this review, we try to briefly summarize the recent advances in mechanoluminescent polymers with the aspects of non-covalent, covalent, and cascade reactions systems. We pay much attention on the applications of such polymer systems in molecular level failure and stress sensors, and give a perspective of their potential applications in novel energy conversion materials and devices, as well as self-healing materials.

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Section: Mechanoluminescent Polymers With Covalent Mechanophoresmentioning

confidence: 99%

Recent advances in mechanoluminescent polymers

Yuan

Chen

2016

Sci. China Mater.

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“…Average values for the Gibbs free energy of stabilization (DG°s tab ) of medium size globular proteins are on the order of 50 kJ mol -1 [76]. With regard to the intrinsic effects, stabilization may involve all levels of the hierarchy of protein structure, local packing of the polypeptide chain, secondary and super secondary structural elements, domains and subunits [77,78]. Hydrogen bonds are favoured at low temperature and become weaker as the temperature is increased.…”

Section: Protein Stability and Intermolecular Interactionsmentioning

confidence: 99%

Protein Folding and Misfolding: A Perspective from Theory

TA¹

2015

J Glycomics Lipidomics

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IntroductionIn appropriate physiological milieu proteins spontaneously fold into their functional three-dimensional structures. The amino acid sequences of functional proteins contain all the information necessary to specify the folds [1,2]. The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu. The wide variety of highly specific structures that result from protein folding and that bring key functional groups into close proximity has enabled living systems to develop astonishing diversity and selectivity in their underlying chemical processes. In addition to generating biological activity, we now know that folding is coupled to many other biological processes, including the trafficking of molecules to specific cellular locations and the regulation of cellular growth and differentiation [3,4].Add to it, correctly folded proteins have long-term stability in crowded biological environments and are able to interact selectively with their natural partners. It is therefore not surprising that the failure of proteins to fold correctly is the origin of a wide variety of pathological conditions [5]. Some concepts, such as energy landscape, Gibbs energy landscape and co-operativity frequently used in the theory of protein folding are examined exactly in one-dimensional systems. It is shown that much of the confusion that exists regarding these, and other concepts arise from the misinterpretation of Anfinsen's thermodynamic hypothesis [6].Moreover, proteins are involved in virtually every biological process and their functions range from catalysis of chemical reactions to maintenance of the electrochemical potential across cell membranes. The molecular conformation of proteins is sensitive to the nature of the aqueous environment [7]. They are synthesized on ribosomes as linear chains of amino acids in a specific order from information encoded within the cellular DNA. To function, it is necessary for these chains to fold into the unique native three dimensional structures that are characteristic for each protein (Figure 1). This involves a complex molecular recognition phenomenon that depends on the cooperative action of many relatively weak non-bonding interactions. As the number of possible conformations for a polypeptide chain is astronomically large, a systematic search for the native (lowest energy) structure would require an almost infinite length of time. Recently, significant progress has been made towards solving this paradox and understanding the mechanism of folding. This has come about through advances in experimental strategies for following the folding reactions of proteins in the laboratory with biophysical techniques, and through progress in theoretical approaches that simulate the folding process with simplified models [8,9].Protein folding is a problem of great importance in both life sciences and biotechnolog...

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“…4A). [4] Glass fibers were modified with an aminosilane layer and enhanced yellow fluorescent protein (eYFP) was covalently bound to the fibers by means of the linker disuccinimidyl terephthalate. The functionalized fibers were embedded into a microdroplet of epoxy resin and then pulled out of the resin using a micromechanical test apparatus.…”

Section: Damage Self-reporting Polymer Compositesmentioning

confidence: 99%

“…[2] Moreover, we will present work on polymeric and protein nanoreactors, [3] and we will review protein-polymer hybrid materials with the capability of selfsensing microdamages. [4] ATRPases Atom transfer radical polymerization (ATRP) is one of the most important synthetic techniques in polymer chemistry of past decades. [5] The steadily increasing number of research articles published on AT RP and related controlled/living radical polymerization techniques is a testimony of the synthetic value of these methods.…”

Section: Introductionmentioning

confidence: 99%

Combining Polymers with the Functionality of Proteins: New Concepts for Atom Transfer Radical Polymerization, Nanoreactors and Damage Self-reporting Materials

Bruns

Lörcher

Makyła

et al. 2013

Chimia

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Proteins are macromolecules with a great diversity of functions. By combining these biomolecules with polymers, exciting opportunities for new concepts in polymer sciences arise. This highlight exemplifies the aforementioned with current research results of our group. We review our discovery that the proteins horseradish peroxidase and hemoglobin possess ATRPase activity, i.e. they catalyze atom transfer radical polymerizations. Moreover, a permeabilization method for polymersomes is presented, where the photoreaction of an α-hydroxyalkylphenone with block copolymer vesicles yields enzyme-containing nanoreactors. A further intriguing possibility to obtain functional nanoreactors is to enclose a polymerization catalyst into the thermosome, a protein cage from the family of chaperonins. Last but not least, fluorescent proteins are discussed as mechanoresponsive molecular sensors that report microdamages within fiber-reinforced composite materials.

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Fluorescent Protein Senses and Reports Mechanical Damage in Glass‐Fiber‐Reinforced Polymer Composites

Cited by 58 publications

References 31 publications

Recent advances in mechanoluminescent polymers

Recent advances in mechanoluminescent polymers

Protein Folding and Misfolding: A Perspective from Theory

Combining Polymers with the Functionality of Proteins: New Concepts for Atom Transfer Radical Polymerization, Nanoreactors and Damage Self-reporting Materials

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