Fabrication of Insoluble Elastin by Enzyme‐Free Cross‐Linking

Abstract: Elastin is an essential extracellular matrix protein that enables tissues and organs such as arteries, lungs, and skin, which undergo continuous deformation, to stretch and recoil. Here, an approach to fabricating artificial elastin with close‐to‐native molecular and mechanical characteristics is described. Recombinantly produced tropoelastin are polymerized through coacervation and allysine‐mediated cross‐linking induced by pyrroloquinoline quinone (PQQ). A technique that allows the recovery and repeated use of PQQ for protein cross‐linking by covalent attachment to magnetic Sepharose beads is developed. The produced material closely resembles natural elastin in its molecular, biochemical, and mechanical properties, enabled by the occurrence of the cross‐linking amino acids desmosine, isodesmosine, and merodesmosine. It possesses elevated resistance against tryptic proteolysis, and its Young's modulus ranging between 1 and 2 MPa is similar to that of natural elastin. The approach described herein enables the engineering of mechanically resilient, elastin‐like materials for biomedical applications.

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch

Erschienen in
Fabrication of Insoluble Elastin by Enzyme‐Free Cross‐Linking ; day:19 ; month:07 ; year:2023 ; extent:13
Macromolecular bioscience ; (19.07.2023) (gesamt 13)

Urheber
Hedtke, Tobias
Mende, Mathias
Steenbock, Heiko
Brinckmann, Jürgen
Menzel, Matthias
Hoehenwarter, Wolfgang
Pietzsch, Markus
Groth, Thomas
Schmelzer, Christian

DOI
10.1002/mabi.202300203
URN
urn:nbn:de:101:1-2023072015240698181505
Rechteinformation
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Letzte Aktualisierung
14.08.2025, 10:49 MESZ

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