Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/smll.200900603 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Protein-polymer bioconjugation, immobilization, and encapsulation: a comparative review towards applicability, functionality, activity, and stability.
Biomater Sci
May 2024
Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, Los Angeles, CA, USA.
Polymer-based biomaterials have received a lot of attention due to their biomedical, agricultural, and industrial potential. Soluble protein-polymer bioconjugates, immobilized proteins, and encapsulated proteins have been shown to tune enzymatic activity, improved pharmacokinetic ability, increased chemical and thermal stability, stimuli responsiveness, and introduced protein recovery. Controlled polymerization techniques, increased protein-polymer attachment techniques, improved polymer surface grafting techniques, controlled polymersome self-assembly, and sophisticated characterization methods have been utilized for the development of well-defined polymer-based biomaterials.
View Article and Find Full Text PDFProtein-supported transition metal catalysts: Preparation, catalytic applications, and prospects.
Int J Biol Macromol
March 2023
Ministry of Education Key Laboratory for the Green Preparation and Application of Functional Materials, Hubei Key Laboratory of Polymer Materials, School of Materials Science and Engineering, Hubei University, Wuhan 430062, China. Electronic address:
The immobilization of transition metal catalysts onto supports enables their easier recycling and improves catalytic performance. Protein supports not only support and stabilize transition metal catalysts but also enable the incorporation of biocompatibility and enzymatic catalysis into these catalysts. Consequently, the engineering of protein-supported transition metal catalysts (PTMCs) has emerged as an effective approach to improving their catalytic performance and widening their catalytic applications.
View Article and Find Full Text PDFMembranized Coacervate Microdroplets: from Versatile Protocell Models to Cytomimetic Materials.
Acc Chem Res
February 2023
Max Planck-Bristol Centre for Minimal Biology, School of Chemistry, University of Bristol, Cantock's Close, BristolBS8 1TS, United Kingdom.
Although complex coacervate microdroplets derived from associative phase separation of counter-charged electrolytes have emerged as a broad platform for the bottom-up construction of membraneless, molecularly crowded protocells, the absence of an enclosing membrane limits the construction of more sophisticated artificial cells and their use as functional cytomimetic materials. To address this problem, we and others have recently developed chemical-based strategies for the membranization of preformed coacervate microdroplets. In this Account, we review our recent work on diverse coacervate systems using a range of membrane building blocks and assembly processes.
View Article and Find Full Text PDFPurification of a Hydrophobic Elastin-Like Protein Toward Scale-Suitable Production of Biomaterials.
Front Bioeng Biotechnol
June 2022
Institute of Process Engineering in Life Sciences, Section IV: Molecular Separation Engineering, Karlsruhe Institute of Technology (KIT), Karlsruhe, Germany.
Elastin-like proteins (ELPs) are polypeptides with potential applications as renewable bio-based high-performance polymers, which undergo a stimulus-responsive reversible phase transition. The ELP investigated in this manuscript-ELP[V2Y-45]-promises fascinating mechanical properties in biomaterial applications. Purification process scalability and purification performance are important factors for the evaluation of potential industrial-scale production of ELPs.
View Article and Find Full Text PDFA Modeling-Based Design to Engineering Protein Hydrogels with Random Copolymers.
ACS Nano
October 2021
Department of Materials Science and Engineering, Northwestern University, Evanston, Illinois 60208, United States.
Protein enzymes have shown great potential in numerous technological applications. However, the design of supporting materials is needed to preserve protein functionality outside their native environment. Direct enzyme-polymer self-assembly offers a promising alternative to immobilize proteins in an aqueous solution, achieving higher control of their stability and enzymatic activity in industrial applications.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!