Study summary · research use only
Site specificity of a catalytic vasoactive intestinal peptide antibody. An inhibitory vasoactive intestinal peptide subsequence distant from the scissile peptide bond
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
This study tested ten fragments of vasoactive intestinal peptide (VIP) for reactivity with a human catalytic autoantibody that cleaves full-length VIP(1-28) at the Gln16-Met17 peptide bond. The authors reported that VIP(15-28), a large COOH-terminal subsequence, was bound by the autoantibody with high affinity (Ki 1.25 nM), while VIP(22-28), a short subsequence distant from the scissile bond, inhibited binding (Ki 242 microM) and hydrolysis (Ki 260 microM) of full-length VIP in a competitive fashion. The autoantibody did not show detectable binding of short VIP subsequences encompassing the scissile bond (VIP(15-21), VIP(11-17), and VIP(13-20)). The authors concluded residues 22-28, located four amino acids distant from the scissile bond, contribute to recognition of VIP by the catalytic autoantibody.
Abstract
Ten fragments of vasoactive intestinal peptide (VIP) were tested for reactivity with a human catalytic autoantibody that cleaves full-length VIP(1-28) at the Gln16-Met17 peptide bond. A large COOH-terminal subsequence, VIP(15-28), was bound by the autoantibody with high affinity (Ki 1.25 nM), suggesting that it is the antibody binding epitope. VIP(22-28), a short subsequence distant from the scissile bond, inhibited the binding (Ki 242 microM) and hydrolysis (Ki 260 microM) of full-length VIP by the catalytic autoantibody in a competitive fashion. The autoantibody did not show detectable binding of short VIP subsequences that encompass the scissile bond (VIP(15-21), VIP(11-17), and VIP(13-20]. These data show that residues 22-28, located four amino acids distant from the scissile bond, contribute in recognition of VIP by the catalytic autoantibody.
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