2003
DOI: 10.1021/bm025671z
|View full text |Cite
|
Sign up to set email alerts
|

Swelling and Mechanical Behaviors of Chemically Cross-Linked Hydrogels of Elastin-like Polypeptides

Abstract: Genetically engineered elastin-like polypeptides consisting of Val-Pro-Gly-X-Gly repeats, where X was chosen to be Lys every 7 or 17 pentapeptides (otherwise X was Val), were synthesized and expressed in E. coli, purified, and chemically cross-linked using tris-succinimidyl aminotriacetate to produce hydrogels. Swelling experiments indicate hydrogel mass decreases by 80-90% gradually over an approximate 50 degrees C temperature range. Gels ranged in stiffness from 0.24 to 3.7 kPa at 7 degrees C and from 1.6 to… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

12
232
0

Year Published

2004
2004
2017
2017

Publication Types

Select...
5
2
1

Relationship

1
7

Authors

Journals

citations
Cited by 254 publications
(244 citation statements)
references
References 23 publications
12
232
0
Order By: Relevance
“…[9][10][11][12][13] Artificial matrices that incorporate functional protein domains have been produced for a variety of applications. [14][15][16][17] The artificial extracellular matrix (aECM) proteins in this study consist of domains derived from elastin and fibronectin ( contains a T7 tag, a heptahistidine tag, an enterokinase cleavage site, and elastin-like domains containing lysine residues for crosslinking. The RGD cell-binding domain is found in aECM 1, whereas the minimal recognition sequence in the RGD cell-binding domain has been scrambled in aECM 2 to provide a negative control.…”
Section: Introductionmentioning
confidence: 99%
“…[9][10][11][12][13] Artificial matrices that incorporate functional protein domains have been produced for a variety of applications. [14][15][16][17] The artificial extracellular matrix (aECM) proteins in this study consist of domains derived from elastin and fibronectin ( contains a T7 tag, a heptahistidine tag, an enterokinase cleavage site, and elastin-like domains containing lysine residues for crosslinking. The RGD cell-binding domain is found in aECM 1, whereas the minimal recognition sequence in the RGD cell-binding domain has been scrambled in aECM 2 to provide a negative control.…”
Section: Introductionmentioning
confidence: 99%
“…27 Expressed proteins were purified from cell lysates using inverse transition cycling (ITC), 34 followed by suspension in 25 mM HEPES-buffered saline and sterile filtration using a low-protein binding 0.22 µm syringe filter (Millex-GV PVDF; Millipore, Billerica, MA). Purified ELPs were concentrated to 200 mg/mL and stored at −80°C until further use.…”
Section: Methodsmentioning
confidence: 99%
“…2228 Further, ELPs are environmentally responsive, as they exhibit an inverse phase transition at a temperature ( T t ), above which they undergo hydrophobic collapse and form a gel-like “aggregated” mass, which enables the synthesis of ELPs that undergo in situ gelling, and may possess a range of properties. 21,23,27,29,30 Physicochemical properties are dependent on the genetic sequence of the ELP, which dictates transition temperature, crosslink density, and responsiveness to other environmental factors, including sensitivity to changes in pH, as well as concentrations of solute and solvent concentrations. ELPs have also been shown not to elicit an immune response when injected subcutaneously.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…Coating of materials with elastin peptides can improve biocompatibility by providing protein sequences required for cell binding (reviewed by (Almine, Bax et al 2010)). Some three dimensional materials formed from elastin-based peptides demonstrate elastin-like properties, including hydrogels that support cell growth and possess high degrees of elasticity (Keeley, Bellingham et al 2002;Trabbic-Carlson, Setton et al 2003). However as with hydrolyzed elastin preparations, synthetic peptides can lack the full repertoire of properties of the fully intact protein and are associated with inflammation (Faury, Ristori et al 1995).…”
Section: Synthetic Elastin-based Peptidesmentioning
confidence: 99%