Results 131 to 140 of about 3,027 (160)

Spectroscopic studies on elastin-like synthetic polypeptides

International Journal of Biological Macromolecules, 1990
Spectroscopic studies on synthetic polypeptides containing the unit-X-G-G (X=V or L) are reported. The sequences, constituting either fragments or model of elastin, were shown to adopt type II beta-turns together with an ensemble of unordered conformations.
M. A. CASTIGLIONE MORELLI, A. SCOPA, A. M. TAMBURRO, GUANTIERI, Valeria   +3 more
openaire   +4 more sources

Epitope tagging for tracking elastin-like polypeptides

Biomaterials, 2006
Elastin-like polypeptides (ELPs) are a class of biocompatible, non-immunogenic and crosslinkable biomaterials that offer promise for use as an injectable scaffold for cartilage repair. In this study, an oligohistidine (His(6)) epitope tag was incorporated at the N-terminus of an ELP using recombinant DNA techniques to permit tracking without ...
Shin R, Ong, Kimberly A, Trabbic-Carlson, Dana L, Nettles, Dong W, Lim, Ashutosh, Chilkoti, Lori A, Setton   +5 more
openaire   +2 more sources

Self-assembled elastin-like polypeptide particles

Acta Biomaterialia, 2008
In this work, the self-assembly of a recombinant elastin-based block copolymer containing both hydrophobic and cross-linking domains from the human elastin protein was investigated. The particle formation and dynamic behavior were characterized using inverted microscopy and dynamic light scattering.
Jill L, Osborne, Robin, Farmer, Kimberly A, Woodhouse   +2 more
openaire   +2 more sources

Catechol-Functionalized Elastin-like Polypeptides as Tissue Adhesives

Biomacromolecules, 2020
Adhesives can potentially be used to achieve fast and efficient wound closure; however, current products show poor bonding on wet surfaces, undergo swelling, and lack adequate biocompatibility. We designed a hydrogel adhesive with recombinant elastin-like polypeptides (ELPs), which are flexible proteins that can be customized for biomedical needs.
Malav S. Desai, Min Chen, Farn Hing Julio Hong, Ju Hun Lee, Yaojiong Wu, Seung-Wuk Lee   +5 more
openaire   +2 more sources

Elastin‐like polypeptides: Biomedical applications of tunable biopolymers

Biopolymers, 2010
AbstractArtificial repetitive polypeptides have grown in popularity as a bioinspired alternative to synthetic polymers. The genetically encoded synthesis, monodispersity, potential lack of toxicity, and biocompatibility are attractive features of these biopolymers for biological applications.
Sarah R Macewan, Ashutosh Chilkoti
exaly   +3 more sources

Graphene-Based Materials Functionalized with Elastin-like Polypeptides

Langmuir, 2014
Graphene-based materials commonly require functionalization for biological applications in order to control their physical/colloidal properties and to introduce additional capabilities, such as stimuli-responsiveness and affinity to specific biomolecules.
Eddie, Wang, Malav S, Desai, Kwang, Heo, Seung-Wuk, Lee   +3 more
openaire   +2 more sources

Elastin‐like polypeptides: A strategic fusion partner for biologics

Biotechnology and Bioengineering, 2016
ABSTRACTElastin‐like peptides (ELPs) are derivatives of tropoelastin with a unique property that allows them to stay soluble below a certain critical temperature but reversibly form aggregates above that temperature. Since they are derived from tropoelastin, ELPs are biocompatible, non‐toxic, and non‐immunogenic. The unique properties of ELPs have made
Agnes, Yeboah, Rick I, Cohen, Charles, Rabolli, Martin L, Yarmush, Francois, Berthiaume   +4 more
openaire   +2 more sources

Molecular Description of the LCST Behavior of an Elastin-Like Polypeptide

Biomacromolecules, 2014
Elastin-like polypeptides (ELPs) with the repeat sequence of VPGVG are widely used as a model system for investigation of lower critical solution temperature (LCST) transition behavior. In this paper, the effect of temperature on the structure, dynamics and association of (VPGVG)18 in aqueous solution is investigated using atomistic molecular dynamics ...
Nan K, Li, Felipe, García Quiroz, Carol K, Hall, Ashutosh, Chilkoti, Yaroslava G, Yingling   +4 more
openaire   +2 more sources

Cononsolvency of Elastin-like Polypeptides in Water/Alcohol Solutions

Biomacromolecules, 2019
Elastin-like polypeptides (ELPs) are one of the most widely-studied classes of protein material because of their lower critical solution temperature (LCST)-like thermoresponsive behavior in aqueous solutions. Here, it is shown that ELPs also exhibit cononsolvency effects, similar to many other water-soluble polymers.
Carolyn E. Mills, Erika Ding, Bradley D. Olsen   +2 more
openaire   +2 more sources

Buffer-Specific Interactions of Imidazolium with Elastin-Like Polypeptides

The Journal of Physical Chemistry B
Buffers are commonly added to protein solutions to stabilize their pH and are typically assumed to not influence any other property of the solution. A series of observations, however, indicate buffer-specific effects on protein stability, suggesting interactions of buffers with proteins.
Julia Keil, Nico F. A. van der Vegt
openaire   +2 more sources