1351556-81-4Relevant articles and documents
Strain Stiffening Hydrogels through Self-Assembly and Covalent Fixation of Semi-Flexible Fibers
Fernandez-Castano Romera, Marcos,Lafleur, René P. M.,Guibert, Clément,Voets, Ilja K.,Storm, Cornelis,Sijbesma, Rint P.
, p. 8771 - 8775 (2017)
Biomimetic, strain-stiffening materials are reported, made through self-assembly and covalent fixation of small building blocks to form fibrous hydrogels that are able to stiffen by an order of magnitude in response to applied stress. The gels consist of
METHOD FOR SYNTHESIS OF PROTEIN AMPHIPHILES
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, (2020/07/14)
The present invention discloses a novel cost effective method for synthesis of protein/peptide amphiphiles irrespective of functional and structural classification of proteins useful in designing a vaccine candidate from antigenic protein. The protein modification of the present invention is universal and hence any protein/peptide can be converted into amphiphilic proteins/peptides.
Rational Design of Supramolecular Dynamic Protein Assemblies by Using a Micelle-Assisted Activity-Based Protein-Labeling Technology
Sandanaraj, Britto S.,Reddy, Mullapudi Mohan,Bhandari, Pavankumar Janardhan,Kumar, Sugam,Aswal, Vinod K.
supporting information, p. 16085 - 16096 (2018/10/15)
The self-assembly of proteins into higher-order superstructures is ubiquitous in biological systems. Genetic methods comprising both computational and rational design strategies are emerging as powerful methods for the design of synthetic protein complexes with high accuracy and fidelity. Although useful, most of the reported protein complexes lack a dynamic behavior, which may limit their potential applications. On the contrary, protein engineering by using chemical strategies offers excellent possibilities for the design of protein complexes with stimuli-responsive functions and adaptive behavior. However, designs based on chemical strategies are not accurate and therefore, yield polydisperse samples that are difficult to characterize. Here, we describe simple design principles for the construction of protein complexes through a supramolecular chemical strategy. A micelle-assisted activity-based protein-labeling technology has been developed to synthesize libraries of facially amphiphilic synthetic proteins, which self-assemble to form protein complexes through hydrophobic interaction. The proposed methodology is amenable for the synthesis of protein complex libraries with molecular weights and dimensions comparable to naturally occurring protein cages. The designed protein complexes display a rich structural diversity, oligomeric states, sizes, and surface charges that can be engineered through the macromolecular design. The broad utility of this method is demonstrated by the design of most sophisticated stimuli-responsive systems that can be programmed to assemble/disassemble in a reversible/irreversible fashion by using the pH or light as trigger.
