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Journal Publication
Title of Article Novel Antimicrobial Peptides from a Cecropin-Like Region of Heteroscorpine-1 from Heterometrus laoticus Venom with Membrane Disruption Activity 
Date of Acceptance 24 September 2021 
Journal
     Title of Journal Molecules 
     Standard SCOPUS 
     Institute of Journal MDPI www.mdpi.com St. Alban-Anlage 66, 4052 Basel, Switzerland  
     ISBN/ISSN 1420-3049 
     Volume 26 
     Issue 19 
     Month October
     Year of Publication 2021 
     Page 5872 
     Abstract The increasing antimicrobial-resistant prevalence has become a severe health problem. It has led to the invention of a new antimicrobial agent such as antimicrobial peptides. Heteroscorpine-1 is an antimicrobial peptide that has the ability to kill many bacterial strains. It consists of 76 amino acid residues with a cecropin-like region in N-terminal and a defensin-like region in the C-terminal. The cecropin-like region from heteroscorpine-1 (CeHS-1) is similar to cecropin B, but it lost its glycine-proline hinge region. The bioinformatics prediction was used to help the designing of mutant peptides. The addition of glycine-proline hinge and positively charged amino acids, the deletion of negatively charged amino acids, and the optimization of the hydrophobicity of the peptide resulted in two mutant peptides, namely, CeHS-1 GP and CeHS-1 GPK. The new mutant peptide showed higher antimicrobial activity than the native peptide without increasing toxicity. The interaction of the peptides with the membrane showed that the peptides were capable of disrupting both the inner and outer bacterial cell membrane. Furthermore, the SEM analysis showed that the peptides created the pore in the bacterial cell membrane resulted in cell membrane disruption. In conclusion, the mutants of CeHS-1 had the potential to develop as novel antimicrobial peptides. 
     Keyword cecropin; CeHS-1; antimicrobial peptide; sequences modification 
Author
617150008-2 Mrs. RIMA ERVIANA [Main Author]
Pharmaceutical Sciences Doctoral Degree

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