Abstract
Antimicrobial activity and self-assembly of the modified TK913 peptide are described. We designed the peptides TK9Z1-4 and TKZ2-3 based on the TK913 sequence and prepared these peptides by Fmoc-SPPS. TKZ3 shows morphology change in the different concentration and potent antimicrobial activities. In addition, TKZ3 has stability in trypsin treatment.
Highlights
Antimicrobial peptides (AMPs) are produced by most living entities to defend against invading organisms
Due to its unique antibacterial method, it is difficult for bacteria to recognize AMPs.[1] more than 5,000 AMPs have been discovered in the past five decades,(2,3) only nine cyclic AMPs have been found for medical use
We report the preparation of the peptide TK913(4) with the negatively charged amino acids on the hydrophilic surface to form high-ordered structure by self-assembly and evaluation of antimicrobial activities
Summary
Antimicrobial peptides (AMPs) are produced by most living entities (microorganisms, animals and plants) to defend against invading organisms. Due to its unique antibacterial method, it is difficult for bacteria to recognize AMPs.[1] more than 5,000 AMPs have been discovered in the past five decades,(2,3) only nine cyclic AMPs have been found for medical use. Most of linear peptides are unstable in the digestive system and it is difficult to use in animal husbandry and industries. Linear peptides are prepared by solid phase techniques and quickly evaluated against antimicrobial activities. The goal of our research is the focus on the improvement of stability of AMPs by forming the rigid secondary structures. We report the preparation of the peptide TK913(4) with the negatively charged amino acids on the hydrophilic surface to form high-ordered structure by self-assembly and evaluation of antimicrobial activities
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