Journal ArticleDOI
Rational Design of Supramolecular Dynamic Protein Assemblies by Using a Micelle-Assisted Activity-Based Protein-Labeling Technology.
Britto S. Sandanaraj,Mullapudi Mohan Reddy,Pavankumar Janardhan Bhandari,Sugam Kumar,Vinod K. Aswal +4 more
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TLDR
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, which is amenable for the synthesis of protein complex libraries with molecular weights and dimensions comparable to naturally occurring protein cages.Abstract:
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.read more
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Redox responsive activity regulation in exceptionally stable supramolecular assembly and co-assembly of a protein
TL;DR: Highly stable redox-responsive supramolecular assembly of a protein Bovine serum albumin which is functionalized with a supramolescular structure directing unit (SSDU) provided excellent protection to the protein against enzymatic hydrolysis as the relative hydroleysis was estimated to be <30% for the co-assembled protein with respect to the free protein under identical conditions.
Journal ArticleDOI
Programmed and Sequential Disassembly of Multi-responsive Supramolecular Protein Nanoassemblies: A Detailed Mechanistic Investigation
TL;DR: A novel chemical method is reported for the construction of multi‐responsive supramolecular nanoassemblies using custom‐designed facially amphiphilic monodisperse protein‐dendron bioconjugates with exquisite control over the disassembly process.
Journal ArticleDOI
Design, Synthesis, and Self‐Assembly Studies of a Suite of Monodisperse, Facially Amphiphilic, Protein–Dendron Conjugates
Britto S. Sandanaraj,Pavankumar Janardhan Bhandari,Mullapudi Mohan Reddy,Akshay Bhagwan Lohote,Bankanidhi Sahoo +4 more
TL;DR: This chemical method discloses a new way to custom‐make monodisperse, facially amphiphilic, protein–dendron bioconjugates, which have the ability to self‐assemble into supramolecular protein nanoassemblies.
Journal ArticleDOI
Rational Design of Semi‐Synthetic Protein Complexes with the Defined Oligomeric State
Britto S. Sandanaraj,Mullapudi Mohan Reddy,Kasuladevu Jagannadha Rao,Pavankumar Janardhan Bhandari +3 more
Journal ArticleDOI
CobT and BzaC catalyze the regiospecific activation and methylation of the 5-hydroxybenzimidazole lower ligand in anaerobic cobamide biosynthesis
TL;DR: This study uses the bza operon from the anaerobic bacterium Moorella thermoacetica to examine the role of CobT and investigate the activity of the first methyltransferase, BzaC, and validate MtBzaC as a SAM:hydroxybenzimidazole-riboside methyl transferase (HBIR-OMT).
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TL;DR: The Iron Core and Hemosiderin, the Iron-A.poferritin Interface, and other Possible Roles for Ferritin are described, as well as other possible alternatives, are described.
Journal ArticleDOI
The coming of age of de novo protein design
TL;DR: De novo protein design explores the full sequence space, guided by the physical principles that underlie protein folding, to design new functional proteins from the ground up to tackle current challenges in biomedicine and nanotechnology.