http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
개별검색 DB통합검색이 안되는 DB는 DB아이콘을 클릭하여 이용하실 수 있습니다.
통계정보 및 조사
예술 / 패션
<해외전자자료 이용권한 안내>
- 이용 대상 : RISS의 모든 해외전자자료는 교수, 강사, 대학(원)생, 연구원, 대학직원에 한하여(로그인 필수) 이용 가능
- 구독대학 소속 이용자: RISS 해외전자자료 통합검색 및 등록된 대학IP 대역 내에서 24시간 무료 이용
- 미구독대학 소속 이용자: RISS 해외전자자료 통합검색을 통한 오후 4시~익일 오전 9시 무료 이용
※ 단, EBSCO ASC/BSC(오후 5시~익일 오전 9시 무료 이용)
Jae-Sung Bae(배재성), Kwang-Ho Jang(장광호), Young-Sam Kwon(권영삼), Hwan-Soo Jang(장환수), Jung-Eun Kim(김정은), Se-Il Park(박세일), Jae-Hyun Lim(임재현), Wen-Xue Li(李文學), Seoung-Jin Lee(이승진) 한국임상수의학회 2003 한국임상수의학회지 Vol.20 No.1
Jae,Sam,Hwang,Hyun,Jeong,Go,Tae,Won,Goo,Su,Il,Seong,Eun,Young,Yun,Mi,Young,Ahn,Seong,Ryul,Kim,Kwan,Ho,Park,Ik,Soo,Kim,Jae,Pil,Jeon,Seok,Woo,Kang 한국잠사학회 2007 International Journal of Industrial Entomology Vol.15 No.1
Insect antimicrobial peptides (AMPs) have been characterized more than 150 peptides since identification of cecropin in the hemolymph of pupae from Hyalophora cecropia in 1980. Therefore, it is considered that insects are good species of AMPs selection. Insect AMPs are small (below 10 kDa), cationic, and amphipathic with variable length, sequence, and structure. They perform a critical role on humoral immunity in the insect innate immune system against invading pathogens such as bacteria, fungi, parasites, and viruses. Most of insect AMPs are induced rapidly in the fat bodies and other specific tissues of insects after septic injury or immune challenge. Then the AMPs subsequently released into the hemolymph to act against microorganisms. These peptides have a broad antimicrobial spectrum against various microorganisms including anticancer activities. Insect AMPs can be divided into four families based on their structures and sequences. That is α-helical peptides, cysteine-rich peptides, proline-rich peptides, and glycine-rich peptides/proteins. For instance, cecropins, insect defensins, proline-rich peptides, and attacins are common insect AMPs, but gloverins and moricins have been identified only in lepidopteran species. In this presentation, we focus on AMPs from insects and discuss current knowledge and recent progresses with potential application of insect AMPs.
To find some antibacterial peptides responsible for bacterial resistance, we performed differential hybridization with total cDNA probes which synthesized from normal and immunized larvae. Thirteen individual cDNA transcripts were expressed differentially in a total 1,862 random cDNA clones. One of upregulated genes is a novel member of the insect defensin-like peptide(Coprisin), a family of antibacterial peptide. Northern blot analysis showed that Coprisin was up-regulated at 4h and reached the highest point level at 16h after injection of E.coli. The deduced amino acid sequence of Coprisin was composed of 80 amino acids with predicted molecular weight of 8.6 kDa and PI of 8.72. Comparison of the deduced amino acid mature portion of Coprisin with defensin-like peptide of other insect indicated that it has 79.1% and 67.4% identity with Anomala cuprea and Allomyrina dichotoma, respectively. To find antibacterial active region of Coprisin, we synthesized four peptides corresponding to amino acid residues 1V-43N-NH2(CopN1), 5-16(CopN2), 19-30(CopN3) and 31-43(CopN4) of coprisin having amidated amino acid residues at their Cterminal. A 12-mer amidated at its C-terminus, ACALHCIALRKK-NH2 (Ala19-Lys30-NH2) was synthesized based on the deduced amino acid sequence, assumed to be an active site sequence. This peptides showed antibacterial activity against E.coli, Staphylococcus aureus, MRSA, Psedomonas syringae, and Pectobacterium carotovorium. Modified 9-mer peptide, LRCIALRKK-NH2, showed strong antibacterial activity than mellitin peptide used as a positive control against gram-negative and gram-positive bacteria. This peptide showed no haemolytic activity and quite stable at 100℃ for several hours of incubation and in a wide pH range(pH2-12). Therefore, this peptide may be a good candidate for the development of new drug with potent antibacterial activity without cytotoxicity.