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The preparation of biotinyl‐ε‐aminocaproylated forms of the vasoactive intestinal polypeptide (VIP) as probes for the VIP receptor
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Vasoactive intestinal polypeptide (VIP) was biotinyl‐ε‐aminocaproylated using sulfosuccinimidyl‐β‐(biotinamido) hexanoate thereby producing a series of products that were separated by high performance liquid chromatography (HPLC). Seven VIP‐derivatives were isolated and the number and location of biotinyl‐ε‐aminocaproylation was determined by a combination of enzymatic degradation and plasma desorption mass spectrometry (PDMS). Receptor binding experiments with the VIP biotinyl‐ε‐aminocaproylated derivatives revealed IC10 values for the monobiotinyl‐ε‐aminocaproylated peptides that were 1.3–3.2 times higher than for natural VIP. All isolated biotinyl‐ε‐aminocaproylated derivatives possess VIP‐like bioactivity as shown by an assay measuring pancreatic juice secretion in cat, VIP biotinyl‐ε‐aminocaproylated in position lysine15 being almost equipotent with natural VIP.
Title: The preparation of biotinyl‐ε‐aminocaproylated forms of the vasoactive intestinal polypeptide (VIP) as probes for the VIP receptor
Description:
Vasoactive intestinal polypeptide (VIP) was biotinyl‐ε‐aminocaproylated using sulfosuccinimidyl‐β‐(biotinamido) hexanoate thereby producing a series of products that were separated by high performance liquid chromatography (HPLC).
Seven VIP‐derivatives were isolated and the number and location of biotinyl‐ε‐aminocaproylation was determined by a combination of enzymatic degradation and plasma desorption mass spectrometry (PDMS).
Receptor binding experiments with the VIP biotinyl‐ε‐aminocaproylated derivatives revealed IC10 values for the monobiotinyl‐ε‐aminocaproylated peptides that were 1.
3–3.
2 times higher than for natural VIP.
All isolated biotinyl‐ε‐aminocaproylated derivatives possess VIP‐like bioactivity as shown by an assay measuring pancreatic juice secretion in cat, VIP biotinyl‐ε‐aminocaproylated in position lysine15 being almost equipotent with natural VIP.
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