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J F Goossens

Publications and source records attributed to J F Goossens.

21 records · Page 2Linked to original sources
PubMed1992

Antagonistic effect of a vasoactive intestinal peptide fragment, vasoactive intestinal peptide(1-11), on guinea pig trachea smooth muscle relaxation.

The conformation of various regions of vasoactive intestinal peptide (VIP) has been analyzed by semiempirical methods, CD, and NMR spectroscopy, indicating that residues 11-21 are most likely to be helical, whereas the amino-terminal portion VIP(1-11) could exhibit two beta-turn structures. VIP(1-11) inhibits 125I-VIP binding to intact guinea pig tracheal epithelial cells and the VIP-induced smooth muscle response. However, the endecapeptide exhibits no effect on the muscle tone. All these data suggest that VIP(1-11) may be a useful tool in studying VIP receptor recognition, its regulation, and cellular functions.

Amino Acid Sequence↗
PubMedDate not supplied

NMR study of five N-terminal peptide fragments of the vasoactive intestinal peptide: crucial role of aromatic residues.

Five peptides related to the N-terminal sequence of the vasoactive intestinal peptide (VIP) have been synthesized. Two-dimensional nuclear magnetic resonance (2D-NMR) experiments (i.e., correlated spectroscopy [COSY]) and low temperature coefficient measurements for particular NH chemical shifts suggest the presence of hydrogen bondings in both VIP (1-7, and VIP (1-11) fragments. Nuclear Over-hauser enhancement spectroscopy (NOESY) show that aromatic interactions stabilize a preferred conformation. The crucial role of the first histidine residue, which is a determinant for the biological activity, is explained by specific interactions with the aromatic protons of Phe6 and Tyr10.

Amides↗