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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived <t>antimicrobial</t> peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .
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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived <t>antimicrobial</t> peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .
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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived <t>antimicrobial</t> peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .
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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived <t>antimicrobial</t> peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .
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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived <t>antimicrobial</t> peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .
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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived <t>antimicrobial</t> peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .
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G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived antimicrobial peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .

Journal: bioRxiv

Article Title: Bridging genomes and peptidomes: hybrid sequencing reveals conserved bioactive peptides in crustaceans

doi: 10.64898/2026.05.04.721987

Figure Lengend Snippet: G e nomic organization and predicted structure of histone-2A-derived peptides in C. sapidus . a) Chromosomal sequence alignment for histone-derived antimicrobial peptide (HDAP), with conserved regions highlighted in yellow and the peptide identified in all tissues highlighted in magenta. b) Superimposed predicted structures of the query (Chr 7) and variant (Chrs 2, 4, 5, 6, 22, and 50) peptide sequences, showing near-identical backbone conformations. Substituted residues in the variant form are highlighted in red. c) Surface mapping of peptide, with red denoting residue deviations which were also highlighted in red in .

Article Snippet: This peptide was recently identified as an antimicrobial peptide with antioxidant activity in the black soldier fly ( Hermetia illucens L. ).

Techniques: Derivative Assay, Sequencing, Variant Assay, Residue