Structural determination of the vasoactive intestinal peptide by two‐dimensional 1H‐nmr spectroscopy

  title={Structural determination of the vasoactive intestinal peptide by two‐dimensional 1H‐nmr spectroscopy},
  author={Yves Th{\'e}riault and Y. Boulancer and Serge St.-Pierre},
The structure of the vasoactive intestinal peptide 1–28 in 40% 2,2,2‐trifluoroethanol was investigated by two‐dimensional 1H‐nmr spectroscopy. All 1H resonances, except the γ, δ, and ε protons of the lysine residues, could be sequentially assigned. Numerous intraresidual as well as short‐range interresidual nuclear Overhauser effect spectroscopy connectivities were observed. Using a variable‐target function minimization, a molecular model consisting of two helical stretches involving residues 7… 

Assessment of the conformational features of vasoactive intestinal peptide in solution by limited proteolysis experiments

It can be concluded that VIP in solution under physiological conditions is characterized by the presence of segments with secondary structure, linked together by “hinge” regions that confer flexibility to the peptide, whereas VIP‐DAP is embedded in a more rigid conformation, more suitable to receptor interaction.

Conformational study of vasoactive intestinal peptide by computational methods.

The conformational profile of vasoactive intestinal peptide (VIP) was characterized using computational methods using simulated annealing in an iterative fashion as the sampling technique and suggests that the common structural features found in VIP(1-11) should also be present in VIP.

Assessment of the Bioactive Conformation of the Vasoactive Intestinal Peptide by Computational Methods

A comparative analysis of the conformational profiles of the segments 1-11 of the native peptide, two VIP antagonists and two inactive analogs is reported, finding the bioactive conformation selected is within a 3 kcal/mol threshold in regard of the respective lowest energy conformation characterized.

Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy.

The correspondence of the global structural features of PACAP with other members of this family of peptides (namely, secretin, glucagon, GHRF1-29 and VIP) is demonstrated by inspection of the chemical shift indices of the alpha-protons.

Enzymatic synthesis of vasoactive intestinal peptide analogs by transglutaminase.

Only one of the three lysine residues of vasoactive intestinal peptide, namely Lys21, was demonstrated to be involved in both inter- and intramolecular cross-link formation.

Novel glycosylated VIP analogs: synthesis, biological activity, and metabolic stability

  • D. DangoorB. Biondi R. Rocchi
  • Biology, Chemistry
    Journal of peptide science : an official publication of the European Peptide Society
  • 2008
Eight glycosylated VIP derivatives were successfully synthesized by the solid‐phase procedure to enhance VIP's metabolic stability and to increase its ligand–receptor binding/activation.

Molecular dynamics (MD) simulations of VIP and PACAP27

Comparison of the structures obtained from the MD trajectories and those derived from the NMR studies in the literature indicates that the GBOBC method is more efficient in the exploration of the conformational space and presents a higher agreement with the experimental structure of VIP and PACAP27 in TFE.

Solution Structure Comparison of the VIP/PACAP Family of Peptides by NMR Spectroscopy

The structural elucidation methodology is described with examples from recent work and general structural conclusions are drawn from data from the now extensive literature.

Experimental study on vasoactive intestinal peptide (VIP) and its diaminopropane bound (VIP-DAP) analog in solution

Structural characterization of VIP by experimental and computational methods as well as a comparative analysis of the peptide with its transglutaminase catalyzed analog VIP-Diaminopropane (VIP-DAP) are reported.



The structure of melittin. A 1H-NMR study in methanol.

The conformation of the 26-residue polypeptide melittin has been studied using 1H-NMR spectroscopy in methanolic solution and the structure is found to be mainly helical, and similar to that found in crystals from diffraction data.

Secondary structure of the human growth hormone releasing factor (GRF 1–29) by two‐dimensional 1H‐nmr spectroscopy

The observation of a large number of α‐amide and amide‐amide interresidual nuclear Overhauser effect connectivities as well as the existence of 11 slowly exchanging amide protons indicates that the peptide adopts a well‐defined secondary structure most likely constituted of a single long helix.

Conformational Analysis of Vasoactive Intestinal Peptide and Related Fragments a

High-resolution NMR spectroscopy has become the most powerful technique for peptide conformational studies in solution, as it can provide direct information about the interactions between various chemical functions of the peptide and the folding pattern of the chain.

Solution structure of an analogue of vasoactive intestinal peptide as determined by two-dimensional NMR and circular dichroism spectroscopies and constrained molecular dynamics.

Structures have been determined for a potent analogue of vasoactive intestinal peptide (VIP), Ac-[Lys12, Lys14, Nle17, Val26, Thr28]VIP (V VIP'), in methanol/water solutions, and the side chains of Asp3, Phe6, Thr7, and Tyr10 are clustered together--these residues are conserved throughout the family of peptide hormones homologous to VIP.

Lipid‐induced conformational changes in glucagon, secretin, and vasoactive intestinal peptide

The helical segment induced by interaction with anionic lipids may play an important physiological role in glucagon, secretin, and vasoactive intestinal peptide.

Isolation from porcine-intestinal wall of a vasoactive octacosapeptide related to secretin and to glucagon.

A polypeptide isolated from porcine upper intestinal wall stimulates exocrine pancreatic secretion in a secretin-like fashion, with an apparent efficiency of 5–10% of that of secretin and also gives rise to hyperglycaemia with about 30% of the efficiency of glucagon.