New preparation and microstructure of the EndoPatch elastin-collagen containing glycosaminoglycans

Lefèbvre, F.; Pilet, Paul; Bonzon, N.; Daculsi, Guy; Rabaud, M.

doi:10.1016/0142-9612(95)00346-0

Cited by 19 publications

(5 citation statements)

References 10 publications

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“…Hydrolyzed soluble elastin has been combined with various materials including collagen[68], glycosaminoglycans [69], calcium phosphate [70], fibrin [71], rhTE [72], and polyethylene glycol terephthalate (PET) [73] to make composites with improved properties for different tissue engineering applications. In our previous study, we found that the addition of rhTE to α-elastin significantly improved the physical properties of rhTE/α-elastin composite scaffolds [72].…”

Section: Elastin As a Biomaterials For Tissue Engineeringmentioning

confidence: 99%

Elastomeric recombinant protein-based biomaterials

Annabi¹,

Mithieux²,

Camci‐Unal³

et al. 2013

Biochemical Engineering Journal

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Elastomeric protein-based biomaterials, produced from elastin derivatives, are widely investigated as promising tissue engineering scaffolds due to their remarkable properties including substantial extensibility, long-term stability, self-assembly, high resilience upon stretching, low energy loss, and excellent biological activity. These elastomers are processed from different sources of soluble elastin such as animal-derived soluble elastin, recombinant human tropoelastin, and elastin-like polypeptides into various forms including three dimensional (3D) porous hydrogels, elastomeric films, and fibrous electrospun scaffolds. Elastin-based biomaterials have shown great potential for the engineering of elastic tissues such as skin, lung and vasculature. In this review, the synthesis and properties of various elastin-based elastomers with their applications in tissue engineering are described.

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Section: Elastin As a Biomaterials For Tissue Engineeringmentioning

confidence: 99%

Elastomeric recombinant protein-based biomaterials

Annabi¹,

Mithieux²,

Camci‐Unal³

et al. 2013

Biochemical Engineering Journal

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“…The cell biological effect chapter 1 elastin as a biomaterial for tissue engineering may be modulated by the amount of solubilised elastin in the scaffold and the extent of crosslinking. Materials based upon α-elastin or elastin fi bres with type I and III collagen can be prepared [149,150], in combination with glycosaminoglycans [151] or calcium phosphate [152]. Elastin preparations combined with fi brin have also been prepared [153].…”

Section: Figure 5 Transmission Electron Micrographs (A C) and Scannmentioning

confidence: 99%

Elastin as a biomaterial for tissue engineering

et al. 2007

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“…The cell biological effect may be modulated by the amount of solubilized elastin in the scaffold and by the extent of crosslinking. Materials based upon k-elastin or elastin fibers with Types I and III collagen can be prepared, 4 in combination with glycosaminoglycans 5 or calcium phosphate. 6 Elastin preparations combined with fibrin have also been achieved.…”

mentioning

confidence: 99%

Structural analysis of some soluble elastins by means of FT‐IR and 2D IR correlation spectroscopy

Popescu¹,

Vasile²,

Crăciunescu

2010

Biopolymers

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Fourier transform infrared (FT‐IR) spectroscopy combined with 2D correlation spectroscopy has been used to offer some information about stability and structure of some soluble elastins. Temperature has been chosen as the perturbation to monitor the infrared behavior of various soluble elastins, namely, α‐elastin p, α‐elastin, and k‐elastin. In the 3800–2700 cm−1 region, the H‐containing groups were analyzed. The bonded hydroxyls are found to decrease prior to the NH‐related hydrogen bonds and also to the conformational reorganization of hydrocarbon chains. The transition temperatures were evaluated and they were found to agree with those obtained from DSC data. The FTIR spectra and their 2nd derivatives denote that α‐ elastins exhibited amide‐I, ‐II and ‐III bands at 1656, 1539 and 1236 cm−1, respectively, while in k‐elastin these bands were found at 1652 cm−1 for amide I, 1540 cm−1 for amide II and 1248 cm−1 for amide III. The macroscopic IR finger‐print method, which combines: general IR spectra, secondary derivative spectra, and 2D‐IR correlation spectra, is useful to discriminate different elastins. Thus using the differences of the position and intensity of the bands from “fingerprint region” of studied elastins, which include the peaks assigned to CO, CC groups from α‐helix, β‐turn, and the peaks assigned to the amide groups, it is possible to identify and discriminate elastins from each others. Furthermore, the pattern of 2D‐IR correlation spectra under thermal perturbation, allow their direct identification and discrimination. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 1072–1084, 2010.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

show abstract

New preparation and microstructure of the EndoPatch elastin-collagen containing glycosaminoglycans

Cited by 19 publications

References 10 publications

Elastomeric recombinant protein-based biomaterials

Elastomeric recombinant protein-based biomaterials

Elastin as a biomaterial for tissue engineering

Structural analysis of some soluble elastins by means of FT‐IR and 2D IR correlation spectroscopy

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