Biomimetic Elastin-Like Polypeptides as Materials for the Activation of Mechanophoric Catalysts

Sebastian Funtan; Anne Funtan; Reinhard Paschke; Wolfgang H. Binder

doi:10.1055/s-0040-1702149

CC BY-NC-ND 4.0 · Organic Materials 2020; 02(02): 116-128
DOI: 10.1055/s-0040-1702149

Original Article

The Author(s). This is an open access article published by Thieme under the terms of the Creative Commons Attribution-NonDerivative-NonCommercial-License, permitting copying and reproduction so long as the original work is given appropriate credit. Contents may not be used for commercial purposes, or adapted, remixed, transformed or built upon. (https://creativecommons.org/licenses/by-nc-nd/4.0/). (2020) The Author(s).

Biomimetic Elastin-Like Polypeptides as Materials for the Activation of Mechanophoric Catalysts

Sebastian Funtan

^aMacromolecular Chemistry, Institute of Chemistry, Faculty of Natural Science II, Martin Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, 06120 Halle (Saale), Germany

,

Anne Funtan

^bBiozentrum, Martin Luther University Halle-Wittenberg, Weinbergweg 22, 06120 Halle (Saale), Germany

,

Reinhard Paschke

^bBiozentrum, Martin Luther University Halle-Wittenberg, Weinbergweg 22, 06120 Halle (Saale), Germany

,

Wolfgang H. Binder

^aMacromolecular Chemistry, Institute of Chemistry, Faculty of Natural Science II, Martin Luther University Halle-Wittenberg, Von-Danckelmann-Platz 4, 06120 Halle (Saale), Germany

› Author Affiliations

Abstract

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Abstract

Elastin-like polypeptides (ELPs) are well known for their elastic and thermoresponsive behaviors. Their elasticity originates from the formation of a β-spiral which is the consequence of stacking type-II β-turns, formed from individual VPGVG pentapeptide units. Here, the synthesis of ELPs of varying chain lengths [VPGVG, (VPGVG)₂, and (VPGVG)₄] and their coupling to a mechanoresponsive catalyst are reported. The attached ELP chains can act as “molecular springs,” allowing for an efficient uptake and transmission of an applied force to the mechanophoric bond. This leads to stress-induced activation of the mechanophoric catalyst, in turn transforming mechanical energy into a “click” reaction. Secondary structure analysis via IR and CD spectroscopy revealed that the β–spiral formation of the ELP is not affected by the coupling process and the β–spiral is still intact in the mechanocatalyst after the coupling. Mechanochemical activation of the synthesized catalysts by an external applied force, studied via ultrasonication, showed conversions of the copper(I)-catalyzed alkyne-azide “click” reaction (CuAAC) up to 5.6% with an increasing chain length of the peptide, proving the potential to incorporate this chemistry into biomaterial engineering.

Key words

Elastin-like polypeptides - β-spiral - peptide coupling - copper(I) - “click” reaction - mechanochemistry - mechanocatalysts

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