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Bradykinin (BK) is a nonapeptide important for several physiological processes such as vasodilatation, increase in vascular permeability and release of inflammatory mediators. BK performs its actions by coupling to and activating the B 2  receptor, a family A G-protein coupled receptor. Using a strategy which allows systematical monitoring of BK R 1  and R 9  residues and B 2  receptor acidic residues Glu 5.35(226)  and Asp 6.58(298) , our study aims at clarifying the BK interaction profile with the B 2  receptor [receptor residue numbers are normalized according to Ballesteros and Weinstein, Methods Neurosci.  25  (1995), pp. 366–428) followed by receptor sequence numbering in brackets]. N- and C-terminal analogs of BK (-A 1 , -G 1 , -K 1 , -E 1  and BK-A 9 ) were tested against wild type B 2 , Glu 5.35(226) Ala and Asp 6.58(298) Ala B 2  mutant receptors for their affinity and capability to elicit responses by mechanical recordings of isolated mice stomach fundus, measuring intracellular calcium mobilization, and competitive fluorimetric binding assays. BK showed 2- and 15-fold decreased potency for Glu 5.35(226)  and Asp 6.58(298)  B 2  mutant receptors, respectively. In B 2 -Glu 5.35(226) Ala BK analogs showed milder reduction in evaluated parameters. On the other hand, in the B 2 -Asp 6.58(298) Ala mutant, no N-terminal analog was able to elicit any response. However, the BK-A 9  analog presented higher affinity parameters than BK in the latter mutant. These findings provide enough support for defining a novel interaction role of BK-R 9  and Asp 6.58(298)  receptor residues.

The role of N-terminal and C-terminal Arg residues from BK on interaction with kinin B 2 receptor