The vasoactive intestinal peptide (VIP) is an ubiquitous peptide of gr
eat potential for applications. Development of new bioactive VIP analo
gs using production in recombinant E coli has been carried out in our
laboratory. This work presents a new multimeric fusion protein express
ing several VIP units separated by factor Xa cleavage site linkers. Th
e steps leading from the affinity purification of the fusion protein a
nd its processing by the factor Xa to the full characterization of the
new bioactive improved VIP analog are also described. (C) Societe fra
ncaise de biochimie et biologie moleculaire/Elsevier, Paris.