Difference between revisions of "Part:BBa K4613010"

 
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<partinfo>BBa_K4613010 short</partinfo>
 
<partinfo>BBa_K4613010 short</partinfo>
  
Elastin-like polypeptides(ELPs) are protein polymers derived from human tropoelastin. One of their key features is that they exhibit phase separation that is often reversible whereby samples remain soluble below a transition temperature(Tt) but form coacervates above Tt. They have many possible applications for sensing, activation, and nano assembly. Furthermore, they are non-immunogenic, substrates for proteolytic biodegradation, and can be decorated with functional peptides, proteins, and small molecules.
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Elastin-like polypeptides (ELPs) are protein polymers derived from human tropoelastin. One of their key features is that they exhibit phase separation that is often reversible whereby samples remain soluble below a transition temperature (Tt) but form coacervates above Tt. They have many possible applications for sensing, activation, and nano assembly. Furthermore, they are non-immunogenic, substrates for proteolytic biodegradation, and can be decorated with functional peptides, proteins, and small molecules.
 
The general structure of polymeric ELPs is (GVGVP)(15&#65289;, where the monomeric unit is Gly-Val-Gly-Val-Pro. The NAU-CHINA 2023 team used this part in versatile model systems for biomaterials development. The polymerization between ELPs containing SpyTags and one containing SpyCatchers can proceed efficiently in a wine production environment.
 
The general structure of polymeric ELPs is (GVGVP)(15&#65289;, where the monomeric unit is Gly-Val-Gly-Val-Pro. The NAU-CHINA 2023 team used this part in versatile model systems for biomaterials development. The polymerization between ELPs containing SpyTags and one containing SpyCatchers can proceed efficiently in a wine production environment.
  
  
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==== Reference ====
 
#Duan T, Li H.In Situ Phase Transition of Elastin-Like Polypeptide Chains Regulates Thermoresponsive Properties of Elastomeric Protein-Based Hydrogels[J].Biomacromolecules,2020, 21 (6): 2258-2267.
 
#Duan T, Li H.In Situ Phase Transition of Elastin-Like Polypeptide Chains Regulates Thermoresponsive Properties of Elastomeric Protein-Based Hydrogels[J].Biomacromolecules,2020, 21 (6): 2258-2267.
 
#Dai Z, Yang X, Wu F, et al.Living fabrication of functional semi-interpenetrating polymeric materials[J].Nat Commun,2021, 12 (1): 3422.
 
#Dai Z, Yang X, Wu F, et al.Living fabrication of functional semi-interpenetrating polymeric materials[J].Nat Commun,2021, 12 (1): 3422.

Latest revision as of 20:39, 10 October 2023


Elastin-like Polypeptide(GVGVP)(15)

Elastin-like polypeptides (ELPs) are protein polymers derived from human tropoelastin. One of their key features is that they exhibit phase separation that is often reversible whereby samples remain soluble below a transition temperature (Tt) but form coacervates above Tt. They have many possible applications for sensing, activation, and nano assembly. Furthermore, they are non-immunogenic, substrates for proteolytic biodegradation, and can be decorated with functional peptides, proteins, and small molecules. The general structure of polymeric ELPs is (GVGVP)(15), where the monomeric unit is Gly-Val-Gly-Val-Pro. The NAU-CHINA 2023 team used this part in versatile model systems for biomaterials development. The polymerization between ELPs containing SpyTags and one containing SpyCatchers can proceed efficiently in a wine production environment.


Reference

  1. Duan T, Li H.In Situ Phase Transition of Elastin-Like Polypeptide Chains Regulates Thermoresponsive Properties of Elastomeric Protein-Based Hydrogels[J].Biomacromolecules,2020, 21 (6): 2258-2267.
  2. Dai Z, Yang X, Wu F, et al.Living fabrication of functional semi-interpenetrating polymeric materials[J].Nat Commun,2021, 12 (1): 3422.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]