King Jay D, Leprince Jérôme, Vaudry Hubert, Coquet Laurent, Jouenne Thierry, Conlon J Michael
Department of Biology, University of Missouri-St. Louis, St. Louis, MO 63121, USA.
Peptides. 2008 Aug;29(8):1287-92. doi: 10.1016/j.peptides.2008.04.005. Epub 2008 May 23.
Peptidomic analysis of norepinephrine-stimulated skin secretions from the Caribbean frog Leptodactylus validus Garman, 1888 led to the identification of three peptides with previously undescribed sequences that were structurally similar to those of antimicrobial peptides isolated from other species of leptodactylid frogs. These paralogs have been termed ocellatin-V1 (GVVDILKGAGKDLLAHALSKLSEKV.NH(2)), ocellatin-V2 (GVLDILKGAGKDLLAHALSKISEKV.NH(2)), and ocellatin-V3 (GVLDILTGAGKDLLAHALSKLSEKV.NH(2)). The very low antimicrobial potency (MIC>200microM) against Escherichia coli and Staphylococcus aureus associated with the peptides is probably a consequence of their lack of amphipathicity and reduced cationicity compared with active members of the ocellatin family from related species.
对1888年加曼氏的加勒比蛙（Leptodactylus validus）去甲肾上腺素刺激的皮肤分泌物进行肽组学分析，结果鉴定出三种具有先前未描述序列的肽，它们在结构上与从其他细趾蟾科蛙类物种中分离出的抗菌肽相似。这些旁系同源物被命名为ocellatin-V1（GVVDILKGAGKDLLAHALSKLSEKV.NH(2)）、ocellatin-V2（GVLDILKGAGKDLLAHALSKISEKV.NH(2)）和ocellatin-V3（GVLDILTGAGKDLLAHALSKLSEKV.NH(2)）。与这些肽相关的对大肠杆菌和金黄色葡萄球菌的抗菌效力非常低（MIC>200μM），这可能是由于与相关物种ocellatin家族的活性成员相比，它们缺乏两亲性且阳离子性降低。
