It is well known that the primary structure of brevinin-2 peptides is greatly diverse in different species and even among different members belonging to the same species ( Conlon et al., 2004 Conlon et al., 2007 Conlon et al., 2008a).
#S AND S CYCLE SKIN#
The first brevinin-2 was identified from the skin of the frog Rana brevipoda porsa ( Morikawa et al., 1992), and more than 80 brevinin-2 peptides, including rugosin A and B, gaegurin 1–3, and nigrocin-1, have been subsequently isolated and identified from different Asian and European rather than North American Ranidae species up to now ( Park et al., 1994 Park et al., 2001 Xu and Lai, 2015). Brevinin-2 is a significant AMP superfamily with extensive structural characteristics and strong biological activities ( Conlon et al., 2004). Currently, according to structural similarity, AMPs found in amphibians have been divided into several peptide families, such as brevinin, esculentin, ranatuerin, cathelicidin, and so on. In conclusion, brevinin-2MP with anti-inflammatory and antimicrobial properties will be an ideal candidate drug molecule for bacterial inflammation treatment.Īntimicrobial peptides (AMPs) in amphibian skin which are encoded by ancient defensive genes play an important role in resisting microbial invasion and have evolved to various structures ( Xu and Lai, 2015). Consistently, brevinin-2MP significantly alleviates the acute inflammatory response in carrageenan-induced mice paw. Furthermore, brevinin-2MP has been found to inhibit the lipopolysaccharide (LPS)-induced expression of pro-inflammatory NO, MCP-1, IL-6, and TNF-α via binding unidentified targets on the cell membrane and consequently suppressing the activation of MAPK/NF-κB signaling cascades induced by LPS in RAW 264.7 cells. Brevinin-2MP (GVITDTLKGVAKTVAAELLRKAHCKLTNSC) with a high amphipathic α-helix in sodium dodecyl sulfate solutions can destroy bacterial cell membrane and kill microbes. Herein a novel AMP named brevinin-2MP has been identified from the skin of the frog Microhyla pulchra by molecular cloning. 2Guangdong Provincial Key Laboratory of New Drug Screening, School of Pharmaceutical Sciences, Southern Medical University, Guangzhou, Chinaīrevinins are an important antimicrobial peptide (AMP) family identified in the skin of Ranidae frogs and generally contain a characteristic ranabox structure at their C-terminal sequence.
1Department of Pulmonary and Critical Care Medicine, Zhujiang Hospital, Southern Medical University, Guangzhou, China.Maolin Tian 1,2 †, Junfang Liu 1 †, Jinwei Chai 2, Jiena Wu 2 and Xueqing Xu 2*