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1H nuclear magnetic resonance determination of the membrane-bound conformation of senktide, a highly selective neurokinin B agonist.

Abstract：

:Senktide is a highly specific and potent analog of neurokinin B, the natural ligand of the tachykinin receptor NK-3. The membrane-bound conformation of senktide, interacting with negatively charged membrane vesicles composed of perdeuterated phosphatidylcholine and phosphatidylglycerol (70:30), has been investigated using two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY). The occurrence of an N-methylated phenylalanine in the peptide's sequence induces a cis-trans-isomerisation of the corresponding peptide bond which is slow on the chemical-shift scale. NMR data indicate a much stronger membrane affinity of the trans isomer, allowing the determination of a highly resolved membrane-bound conformation using distance geometry and energy minimization. The membrane-bound backbone conformation of several residues is found to be close to a left-handed helix, certainly due to the presence of nonnatural residues (succinylated N-terminal, N-methyl-phenylalanine) as well as a glycine. The results are discussed in the context of a possible biological relevance of the membrane-bound conformation, in terms of the affinity and specificity of this neuropeptide.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Bersch B,Koehl P,Nakatani Y,Ourisson G,Milon A

doi

10.1007/BF00176010

subject

Has Abstract

pub_date

1993-07-01 00:00:00

pages

443-61

issue

4

eissn

0925-2738

issn

1573-5001

journal_volume

3

pub_type

杂志文章

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