Assembly of transmembrane pores from mirror-image peptides

Nature Communications   September 14, 2022|

Smrithi Krishnan R, Kalyanashis Jana, Amina H. Shaji, Karthika S. Nair, Anjali Devi Das, Devika Vikraman, Harsha Bajaj, Ulrich Kleinekathöfer & Kozhinjampara R. Mahendran


Tailored transmembrane alpha-helical pores with desired structural and functional versatility have promising applications in nanobiotechnology. Herein, we present a transmembrane pore DpPorA, based on the natural pore PorACj, built from D-amino acid α-helical peptides. Using single-channel current recordings, we show that DpPorA peptides self-assemble into uniform cation-selective pores in lipid membranes and exhibit properties distinct from their L-amino acid counterparts. DpPorA shows resistance to protease and acts as a functional nanopore sensor to detect cyclic sugars, polypeptides, and polymers. Fluorescence imaging reveals that DpPorA forms well-defined pores in giant unilamellar vesicles facilitating the transport of hydrophilic molecules. A second D-amino acid peptide based on the polysaccharide transporter Wza forms transient pores confirming sequence specificity in stable, functional pore formation. Finally, molecular dynamics simulations reveal the specific alpha-helical packing and surface charge conformation of the D-pores consistent with experimental observations. Our findings will aid the design of sophisticated pores for single-molecule sensing related technologies.


Rajiv Gandhi Centre for Biotechnology (RGCB),
Thycaud Post, Poojappura,
Thiruvananthapuram - 695 014, Kerala, India
+91-471-2529400 | 2347975 | 2348753

My Gov Prime Ministers National Relife Fund India Gov Make In India Make In India Data gov in

Last Updated on: September 27, 2023
CERT-In Certified Website