환경오염이 심각해짐에 따라 국내외적으로 환경에 대한 관심이 고조되고 인체에 해를 끼치는 환경요인으로부터 방어하기 위한 많은 노력들이 기울여지고 있다. 특히 내분비계장애물질이 생식기능과 면역기능을 약화시키고, 행동 이상을 일으키며, 암 발생률을 높인다는 점이 밝혀지기 시작하면서 많은 연구들이 발표되고 여러 가지 방법들이 내분비계장애물질과 더불어 환경분야연구에 응용되어왔지만 단백질을 대상으로 연구하여 유전자기능을 연구하는 프로테오믹스(proteomics)

Toxic Mastoparan B(MP-B) which is purified from the venom of the hornet Vespa basalis is a cationic amphiphilic tetradecapeptide. MP-B and its Ala-substituted analogues were synthesized by solid phase method and the toxic peptide-membrane interactions were examined by circular dichroism(CD) spectra, fluorescence spectra, and leakage abilities in phospholipid membranes. In the presence of phospholipid vesicles, synthetic MP-B and its analogues formed amphiphilic α-helical structures, but in the buffer solution, those exhibited random coil conformation as measured by CD. Fluorescence spectra of MP-13 and its analogues which indicated the binding affinity of peptide on phospholipid vesicles showed that the replacement of Lys at position 2 and 11 with Ala caused a remarkable effect in the blue shift and that at position 2, in the leakage ability of the peptide.