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International Journal of Spectroscopy
Volume 2011 (2011), Article ID 296256, 8 pages
Research Article

The Conformation and Assignment of the Proton NMR Spectrum in Water of DX600, a Bioactive Peptide with a Random Coil Conformation

Chemistry Department, Pomona College, Claremont, CA 91711, USA

Received 7 November 2010; Revised 16 January 2011; Accepted 1 February 2011

Academic Editor: Stefan Schmatz

Copyright © 2011 Wayne E. Steinmetz et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


DX600, a small peptide with 26 residues, is a potent, highly selective inhibitor of angiotensin converting enzyme 2 (ACE2). A range of NMR methods including TOCSY and ROESY yield an assignment of its proton spectrum in water and constraints on its conformation. Constrained molecular dynamics simulations of solvated DX600 show that the peptide's most abundant conformer adopts a predominantly random coil conformation. Constrained by the disulfide bond, its backbone defines an overhand knot with frayed ends.