Results 171 to 180 of about 14,557 (201)
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Self-assembled elastin-like polypeptide particles
Acta Biomaterialia, 2008In 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 +2 more
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Catechol-Functionalized Elastin-like Polypeptides as Tissue Adhesives
Biomacromolecules, 2020Adhesives 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 +5 more
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Graphene-Based Materials Functionalized with Elastin-like Polypeptides
Langmuir, 2014Graphene-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 +3 more
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Elastin‐like polypeptides: A strategic fusion partner for biologics
Biotechnology and Bioengineering, 2016ABSTRACTElastin‐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 +4 more
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Molecular Description of the LCST Behavior of an Elastin-Like Polypeptide
Biomacromolecules, 2014Elastin-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 +4 more
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Cononsolvency of Elastin-like Polypeptides in Water/Alcohol Solutions
Biomacromolecules, 2019Elastin-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 +2 more
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Elastin‐like polypeptides: Biomedical applications of tunable biopolymers
Peptide Science, 2010AbstractArtificial 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
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Buffer-Specific Interactions of Imidazolium with Elastin-Like Polypeptides
The Journal of Physical Chemistry BBuffers 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
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Coacervation of Elastin-Like Polypeptides: A Coarse-Grained Perspective
Journal of Chemical Theory and ComputationElastin-like polypeptides (ELPs) are a class of bioengineered polymers that mimic the hydrophobic repeat units of the precursor of the elastin protein. These segments drive self-aggregation, a process influenced by various stimuli such as temperature, pH, salt concentration, hydrophobicity of guest amino acid residues, etc.
Piyali Mukherjee +2 more
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Protease-Driven Phase Separation of Elastin-Like Polypeptides
BiomacromoleculesElastin-like polypeptides (ELPs) are a promising material platform for engineering stimuli-responsive biomaterials, as ELPs undergo phase separation above a tunable transition temperature. ELPs with phase behavior that is isothermally regulated by biological stimuli remain attractive for applications in biological systems.
Brendan M. Wirtz +4 more
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