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Biophysical Journal 85:4002-4011 (2003)
© 2003 The Biophysical Society

Three-Dimensional Structure of the Mammalian Tachykinin Peptide Neurokinin A Bound to Lipid Micelles

Indu R. Chandrashekar and Sudha M. Cowsik

School of Life Sciences, Jawaharlal Nehru University, New Delhi 110 067, India

Correspondence: Address reprint requests to Sudha M. Cowsik, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110 067, India. Tel.: 91-11-26177359 or 91-11-26170016; Fax: 91-11-26165886 or 91-11-26187338; E-mail: scowsik{at}yahoo.com.

The solution structure of NKA, a decapeptide of mammalian origin, has been characterized by CD spectropolarimetry and 2D proton nuclear magnetic resonance (2D 1H-NMR) spectroscopy in both aqueous and membrane mimetic solvents. Unambiguous NMR assignments of protons have been made with the aid of correlation spectroscopy (DQF-COSY and TOCSY) experiments and nuclear Overhauser effect spectroscopy (NOESY and ROESY) experiments. The distance constraints obtained from the NMR data have been utilized to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that in water NKA prefers to be in an extended chain conformation whereas a helical conformation is induced in the central core and the C-terminal region (D4-M10) of the peptide in the presence of perdeuterated dodecylphosphocholine (DPC) micelles, a membrane model system. Though less defined the N-terminus also displays some degree of order and a possible turn structure. The conformation adopted by NKA in the presence of DPC micelles represents a structural motif typical of neurokinin-2 selective agonists and is similar to that reported for eledoisin in hydrophobic environment.






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Copyright © 2003 by the Biophysical Society.