Sequence Analysis and Modeling of Antimicrobial Peptide from Goat Milk Protein Hydrolyzed by Bromelain

Eni Kusumaningtyas, Raphaella Widiastuti, H D Kusumaningrum, M T Suhartono

Abstract


Hydrolysis of goat milk protein by bromelain generates fractions <10 kDa which act as antimicrobe. The fractions contain some peptides that not all were biologically active. Sequence analysis and modeling of the peptides sequences are important to predict their potential bioactivities. The aims of this study were to obtain physicochemical and structure prediction of peptides and their relation with antimicrobial activity. The study was conducted by sequencing of selected fraction in the electrophoresis gel, analyzing and modeling. Analysis of the peptide showed that peptide VLVLDTDYK that predicted from β-lactoglobulin sequence had similar sequence with antimicrobial peptide indolicidin which active to Gram positive bacteria. Peptide LVNELTEFAK was potent to be antimicrobial peptide with therapeutic index 28.69. Modeling of the peptide showed that peptide LVNELTEFAK was able to form helix which important for interaction with microbial membrane. Replacing 2nd amino acid Valine (V) to Alanine (A) and 4th amino acid Glutamic acid (E) to Serine (S) might able to increase the therapeutic index to 94.91. Based on the result, peptide LVNELTEFAK potent to be antimicrobial peptide and replacing certain amino acid was able to increase therapeutic index and its antimicrobial activity.

Keywords


Sequence; Analysis; Modeling; Antimicrobial Peptide

References


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DOI: 10.14334/Proc.Intsem.LPVT-2016-p.327-335

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