Antimicrobial peptides (AMPs) are biologically dynamic molecules produced by all type of organisms as a fundamental component of their innate immune system. The present study deals with the identification of a histone H2A-derived antimicrobial peptide, Hipposin from mangrove whip ray, Himantura walga. A 243 base pair fragment encoding 81 amino acid residues amplified from complementary DNA was identified as Hipposin and termed as Hw-Hip. Homologous analysis showed that Hw-Hip belongs to the Histone H2A superfamily and shares sequence identity with other histone-derived AMPs from fishes. Phylogenetic analysis of Hw-Hip displayed clustering with the fish H2A histones. Secondary structure analysis showed the presence of three α-helices and four random coils with a prominent proline hinge. The physicochemical properties of Hw-Hip are in agreement with the properties of antimicrobial peptides. A 39-mer active peptide sequence was released by proteolytic cleavage in silico. Functional characterisation of active peptide in silico revealed antibacterial, anticancer and antibiofilm activities making Hw-Hip a promising candidate for further exploration.

抗菌肽 (AMP) 是由所有类型的生物体产生的生物动态分子，是其先天免疫系统的基本组成部分。本研究涉及从红树林鞭鳐Himantura walga 中鉴定组蛋白 H2A 衍生的抗菌肽Hipposin。从互补DNA扩增的编码81个氨基酸残基的243个碱基对片段被鉴定为Hipposin并称为Hw- Hip。同源分析表明Hw -Hip 属于组蛋白 H2A 超家族，与来自鱼类的其他组蛋白衍生的 AMP 具有序列同一性。Hw的系统发育分析-臀部显示与鱼 H2A 组蛋白的聚类。二级结构分析显示存在三个α-螺旋和四个具有突出脯氨酸铰链的无规卷曲。Hw -Hip的理化特性与抗菌肽的特性一致。39-mer 活性肽序列通过计算机蛋白水解裂解释放。计算机活性肽的功能表征揭示了抗菌、抗癌和抗生物膜活性，使Hw- Hip 成为进一步探索的有希望的候选者。