Study of molecular design for antagonisting C5a anaphylatoxin
LU Feng-lin
ZHU Xi-hua
ZHENG ping
Abstract：Objective To discover high hydrophilic profiles of the human C5a receptor(CD88) and the specific high-
affinity binding site for its ligand C5a anaphylatoxin form relationship between the structure and function of the protein and
the protein molecular design principles. Methods The peptides were synthesized by 431A automatic peptide synthesizer,puri-
fied by high pressure liquid phase chromatography (HPLC) and confirmed by capillary electrophoresis. Results The N-termi-
nus No. 9～30 profile of the C5aR (called as P22) could interact with anti-C5aR McAb (S5/1,from Serotic Co.),as deter-
mined by ELISA. Furthermore,it could also inhibit OD490 values remarkably by 10.0 μg/L rhC5a(P＜0.05). In addition,the
elevation of cytoplasmic Ca2+ concentration induced by 10.0μg/L rhC5a was inhibited by P22 in dt2cAMP differentiated U937
cells(P＜0.01). Conclusion It is possible that the C5a anaphylatoxin could be removed from the body,and some new types of
drug which could be used to treat diseases related to C5a anaphylatoxin could be manufactured.
Keywords：molecular designC5a anaphylatoxinC5a receptor(CD88)
Publication Date：2000-01-01
Online Publishing Date：2025-08-15(First online date of this platform, not the publication date of the document)
Pages：6( 401-406 )