Bee venom contains a variety of peptide constituents, including low-molecular-weight protease inhibitors. While the putativelow-molecular-weight serine protease inhibitor Api m 6 containing a trypsin inhibitor-like cysteine-rich domain was identifiedfrom honeybee (Apis mellifera) venom, no anti-fibrinolytic or anti-microbial roles for this inhibitor have been elucidated.In this study, we identified an Asiatic honeybee (A. cerana) venom serine protease inhibitor (AcVSPI) that was shownto act as a microbial serine protease inhibitor and plasmin inhibitor. AcVSPI was found to consist of a trypsin inhibitor-likedomain that displays ten cysteine residues. Interestingly, the AcVSPI peptide sequence exhibited high similarity to the putativelow-molecular-weight serine protease inhibitor Api m 6, which suggests that AcVSPI is an allergen Api m 6-like peptide.Recombinant AcVSPI was expressed in baculovirus-infected insect cells, and it demonstrated inhibitory activity against trypsin,but not chymotrypsin. Additionally, AcVSPI has inhibitory effects against plasmin and microbial serine proteases; however,it does not have any detectable inhibitory effects on thrombin or elastase. Consistent with these inhibitory effects, AcVSPIinhibited the plasmin-mediated degradation of fibrin to fibrin degradation products. AcVSPI also bound to bacterial andfungal surfaces and exhibited anti-microbial activity against fungi as well as gram-positive and gram-negative bacteria. Thesefindings demonstrate the anti-fibrinolytic and anti-microbial roles of AcVSPI as a serine protease inhibitor.

Bee venom contains a variety of toxic components, including vitellogenin, which display various biological, toxicological,and pharmacological activities. However, the biological actions of vitellogenin, a venom protein in bee venom, remainlargely unknown. Here, we demonstrate that Asiatic honeybee (Apis cerana) venom vitellogenin (AcV-Vg) exhibits anti-oxidantand anti-microbial activities. AcV-Vg is expressed in the venom gland and is then secreted into venom. The recombinantAcV-Vg protein was produced in baculovirus-infected insect cells. We found that AcV-Vg reduced cytotoxicity and oxidativedamage against oxidative stress. Furthermore, AcV-Vg bound to microbial surfaces and induced structural damage in themicrobial cell walls, which, in turn, exhibited anti-microbial activity against bacteria and fungi. Together, our data demonstratedthat the bee venom protein AcV-Vg has multifunctional roles as an anti-oxidant and anti-microbial agent.

Bee venom contains a variety of peptide constituents that have various biological, toxicological, and pharmacological actions. However, the biological actions of secapin, a venom peptide in bee venom, remain largely unknown. Here, we provide the first evidence that the Asiatic honeybee (Apis cerana) secapin (AcSecapin-1) exhibits anti-fibrinolytic, anti-elastolytic, and anti-microbial activities. AcSecapin-1 functions as a serine protease inhibitor-like peptide that has inhibitory effects against plasmin, elastases, microbial serine proteases, trypsin, and chymotrypsin. Consistent with these functions, AcSecapin-1 inhibited the plasmin-mediated degradation of fibrin to fibrin degradation products, thus indicating the role of AcSecapin-1 as a clotting factor. AcSecapin-1 also inhibited both human neutrophil and porcine pancreatic elastases. Furthermore, AcSecapin-1 exhibited anti-microbial activity against fungi and Gram-positive and Gram-negative bacteria. Taken together, our data demonstrated that AcSecapin-1 has a multifunctional role as an anti-fibrinolytic agent, an anti-elastolytic agent, and an anti-microbial peptide, and our data suggested novel functions for the biological actions of the bee venom peptide, secapin.

This study was performed to develop a new natural antimicrobial materials by analyzing the effect of extracts obtained from Ten Lauraceae Species on the inhibitory activity against Propionibacterium acnes. The plant materials were collected from Wando and Jeju islands, and the antimicrobial activity of the crude extracts was examined by the agar diffusion method with different part (i.e., leaf and branch), solvents (i.e., distilled water, 80% ethanol, and 100% methanol) and at different ultrasonic extracting times (i.e., 15, 30, and 45 minutes). The control agents used were synthetic antimicrobials, methylparaben and phenoxyethanol, at concentrations of 0.4, 1, 2, and 4 ㎎/disc. Altogether, extracts of 10 species used in the study showed inhibitory activity, which confirmed their antimicrobial action against acnes. Among these, leaves of Laurus nobilis L. which was extracted in 80% ethanol for 45 min showed the largest clear zone (19.8 ㎜). Leaves of L. nobilis L., showing highest antimicrobial activities among 10 species, were successively reextracted with n-hexane, chloroform, ethylacetate and n-butanol. As a results, in all fractions except butanol, clear zone above 10 ㎜ were formed. The ethyl acetate fraction showed the highest inhibitory activity (13.3 ㎜) and the inhibitory activity was significantly higher than that of crude extract (10.2 ㎜) and phenoxyethanol as a control (12.5 ㎜).

스프레이 국화의 용도 다양화 측면에서 ‘금방울’, ‘매직볼’, ‘핑크팡팡’ 꽃잎을 수확하여 열수 및 에탄올 추출물의 생리활성 효과를 조사하였다. 총 페놀함량은 chlrogenic acid를 표준물질로 했을 때 열수 추출물에서는 ‘금방울’(100.1mg·L-1), ‘핑크팡팡’(66.4mg·L-1), ‘매직볼’(52.9mg·L-1)순으로, 에탄올 추출물에서는 ‘매직볼’ (95.7mg·L-1), ‘핑크팡팡’(65.1mg·L-1), ‘금방울’(49.4mg·L-1) 순으로 많았다. 플라보노이드 함량은 열수 추출물은 ‘핑크팡팡’에서 45.7mg·L-1로, 에탄올 추출물에서는 ‘매직볼’이 54.0mg·L-1로 가장 많았다. 전자공여능에서 IC50값은 열수 추출물과 에탄올 추출물 모두 ‘매직볼’에서 각각 166.0 및 112.7mg·L-1로 가장 낮게 나타나 효과적이었다. 아질산염 소거능은 IC50값을 고려할 때 열수 추출물에서는 ‘핑크팡팡’(112.1mg·L-1)이, 에탄올 추출물에서는 ‘매직볼’(105.3mg·L-1)이 효과적이었다. 항균활성은 ‘매직볼’의 에탄올 추출물이 그람양성균인 Bacillus subtilis와 그람음성균인 Salmonella enteritidis에 대해 높은 활성을 나타냈다. 결론적으로 '매직볼'의 생리활성효과가 좋은 것으로 나타났으며, 스프레이 국화의 품종 간에 생리활성 차이가 있는 것이 확인되었다. 따라서 금후 스프레이 국화의 용도 확대와 이용성 향상 측면에서 각각의 품종에 대한 생리활성 효과 구명이 필요하다.