the conformation and assignment of the proton nmr spectrum in water of dx600, a bioactive peptide with a random coil conformation的构象和分配水的质子核磁共振谱dx600,生物活性肽和无规卷曲构象.pdfVIP

Hindawi Publishing Corporation International Journal of Spectroscopy Volume 2011, Article ID 296256, 8 pages doi:10.1155/2011/296256 Research Article The Conformation and Assignment of the Proton NMR Spectrum in Water of DX600, a Bioactive Peptide with a Random Coil Conformation Wayne E. Steinmetz, Timothy N. Carrell, and Richard B. Peprah Chemistry Department, Pomona College, Claremont, CA 91711, USA Correspondence should be addressed to Wayne E. Steinmetz, wsteinmetz@ 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. 1. Introduction as tools for exploring and modulating its biological function [10, 11]. Huang et al. screened peptide libraries displayed Angiotensin converting enzyme (ACE), a dipeptidase, is a key on phage and identified six highly potent inhibitors of component of the renin-angiotensin system