Design and Assembly of Transmembrane Helix Barrel
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UP-AND-COMING SCIENTIST
Design and Assembly of Transmembrane Helix Barrel Kozhinjampara R. Mahendran1 Received: 28 August 2020 / Accepted: 8 October 2020 © Springer Science+Business Media, LLC, part of Springer Nature 2020
Graphic Abstract
Introduction by Amitabha Chattopadhyay, Section Head Editor It gives me great pleasure to introduce the following commentary by Dr. Kozhinjampara R. Mahendran, featured as an Up-and-Coming Scientist in the present issue of the Journal of Membrane Biology. Dr. Mahendran holds a Ph.D. in Biochemical Engineering from the Jacobs University Bremen, Germany (Thesis Supervisor: Prof. Mathias Winterhalter) and pursued an initial postdoctoral research stint in a joint collaboration of the Jacobs University Bremen, Germany and the University of Cambridge, UK. Subsequently, he carried out further postdoctoral research in the laboratory of Prof. Hagan Bayley at the University of Oxford, UK, where he demonstrated the fabrication of a novel monodisperse transmembrane α-helical peptide barrel (Mahendran et al. 2017). This breakthrough introduced an exciting dimension to the development of sensors based on membrane proteins, which has been conventionally templated on β-barrel scaffolds. Dr. Mahendran joined the Rajiv Gandhi Centre for
* Kozhinjampara R. Mahendran [email protected]
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Membrane Biology Laboratory, Interdisciplinary Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram 695014, India
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K. R. Mahendran
Biotechnology, Thiruvananthapuram, India as a DBT-Ramalingaswamy Faculty Fellow in September 2016, where he set up an independent research group working on design principles of sensors and actuators templated on membrane proteins. This commentary offers an overview of emerging paradigms in the field of transmembrane protein sensors, with an emphasis on the challenges and excitements inherent in the adaptation of α-helical transmembrane proteins and peptides to these applications. Work from his group (Satheesan and Mahendran 2018; Krishnan et al. 2019; Puthumadathil et al. 2019; Vikraman et al. 2020) has established designer α-helical peptide barrels as powerful models for unraveling the grammar of membrane protein folding and viable alternatives for engineering single-molecule sensors and peptide-based therapeutics.
Introduction Membrane-spanning proteins account for one-third of all proteins across all genomes involved in regulating the transport of a wide variety of molecules such as nutrients, ions, drugs and biomolecules into the cells (Nikaido 2003, Bayley and Jayasinghe 2004, Pages et al. 2008, Dal Peraro and van der Goot 2016). The majority of natural membrane proteins are α-helical and usually hydrophobic or amphipathic (von Heijne 2006; Bayley 2009). Redesigning membrane proteins is one of the main approaches within the engineering field to modify proteins into useful biomaterials for applications in biotechnology (Bayley and Jayasinghe 2004; Majd et al. 2010; Aksoyoglu et al. 2016; Ayub and Bayley 2016; Kasianowicz
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