Design Antibacterial Peptide Based On Lactoferrin And Its Bio-effects

In view of the current antimicrobial drug resistance with enhanced, especially the abuseof antibiotics has become increasingly serious,Human beings need to develop a kind of newtype high efficiency, low toxicity and no residual antimicrobial agents. Antibacterial peptidehas wide antimicrobial spectrum, stability, the advantages of small side effect, no drugresistance, is expected to overcome the current antimicrobial drug resistance is strong, largeside effects such as series of problems. At present, the existing variety of antibacterial activitypeptide molecular design and retrofit methods were used in the study of antibacterial peptides,is expected to improve the activity of antibacterial and its stability in plasma, at the same time,reduce the side effects, thus lay a foundation for antimicrobial peptide in clinical application.Although existing antibacterial peptide molecular transformation has made gratifying progress,but there are many problems in antibacterial activity, chemical synthesis, cell toxicity,especially resistance to digestion, etc.Based on the current research status, This article makes reference to the design concept ofsmall molecule cationic antimicrobial peptides，Retain its "short peptides, high charge,amphiphilic more powerful advantages amino acids," and introduced the advantages of thedesign method of natural amino acidat the same time.The virtual combinatorial designs andhigh-throughput screening of antimicrobial peptides were performed by using quantitativestructure-activity relationship (QSAR) method based on the template cationic antimicrobialpeptides LfcinB64-9(RRWQWR),and taking into account the sequence requirements ofantimicrobial peptides mode,the amino structure of the dominant sites and its chemcialstructural modification.The detail as following：1、Analysis the antibacterial peptide level sequence alignment to the existing antibacterialpeptide database (APD2), determine the cationic antimicrobial peptide sequence mode.2、Existing cationic antimicrobial peptide for quantitative structure-activity relationshipstudies, determine the core advantage of amino acid sequence and method of chemical modification.3、The virtual structure diversity of antimicrobial peptide library based on LfcinB64-9andsequence model, advantage point of amino acids and their chemically modified.4、Filter and synthesis the peptides based on the structure-activity relationship analysis;5、By determine its antimicrobial activity, Plasma stability and cell toxicity, check out thethe best design of the antibacterial peptide, In preparation for the next became a drug.The experimental results show that The introduction of non-natural amino acidmodification transformation "short peptide chain, charge, amphiphilic advantage amino acidsmall molecule cationic antimicrobial peptides of the design concept and the design method ofvirtual combinatorial, can not only be based on the rational design of the structure-activityrelationship research the structural diversity of polypeptide molecules, and effectively improvethe screening effect, reduce research costs. Its antimicrobial activity is expected to furtherimprove and solve the problem of scale production of antimicrobial peptides to clinicalpractice has important theoretical research value.