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Studies on the Effect of Heilicity of α-helical Peptides on Their Biological Activities

Author: HeLiYan
Tutor: ChenYuXin
School: Jilin University
Course: Biochemistry and Molecular Biology
Keywords: biological activity of alpha - helical peptide Helicity Anti - virus Anti-cancer Anti-bacterial
CLC: Q51
Type: Master's thesis
Year: 2011
Downloads: 53
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Abstract

Membrane active peptide is bioactive peptides in a Cat is derived from in vivo genome encodes or in vitro chemical synthesis of a class having the polypeptide molecules, specific recognition and removal of the diseased cells in the body can withstand exogenous factor against. Membrane active peptide having a smaller molecular weight, generally composed of 12-100 amino acids, a class of small peptide molecules. At present, the study of membrane active peptide has become a research hotspot in the worldwide, has great application prospects. Which comprises a highly effective broad spectrum antibacterial activity of antimicrobial peptides; having a good specific the anticancer peptide (specificity can not only kill cancer cells, while not toxic to normal cells) as well as the antiviral peptide on tumor cells. amphiphilic alpha-helical cationic peptide is a large class of membrane active peptide in a hydrophobic environment, such polypeptides can be induced by the typical alpha-helical structure and amphipathic, i.e. having the complete hydrophobic surface and the pro the water; under physiological conditions or under neutral pH conditions, the net charge of the polypeptide molecule is positively charged, it is called cationic peptides, is to study the most widely used class of biologically active peptides. Alpha-helical amphiphilic cationic membrane active peptides have been extracted from the initial active peptide preparation and study of factors affecting the activity into a more in-depth level, the study of the active mechanism. Researchers through a unique research methodology, the diverse research strategy in many ways, multi-angle for this type of active peptides comprehensive and in-depth interpretation, in order to expect to find more and better used in clinical cell membrane active peptides, is committed to in to contribute to human health. Structural parameters affect the activity of membrane-active peptide helicity amphiphilic, hydrophobicity, charge number, self-interaction, the subject will have an impact factors - helicity study to illustrate the structure and function of the relationship between the molecular design and renovation of the structure-activity relationship of a-helix active peptide can play a guiding role, and can be used to filter with high activity and low toxicity of membrane active peptides. Polypeptide design, raise or lower the helicity of the polypeptide amino acid substitution method. The polypeptide molecules helicity content in different media can be used circular dichroism spectroscopy to determine the. The polypeptide molecule hydrophobic reversed-phase high-performance liquid chromatography to determine the. The polypeptide molecules self-interaction measured by RP-HPLC temperature monitoring technology to achieve. By their resistance assay for HCV proliferation and experimental infection of HIV virus and anti-viral polypeptide antiviral activity; using the MTT method of determination of the type of anticancer peptides inhibit the killing effect on Hela; by their ability to inhibit bacterial detection experiments detect antimicrobial peptides anti-bacterial ability. Membrane active peptide toxicity to normal cells ability to measure the red blood cells of polypeptide cleavage; selectivity of the membrane active peptide Analyzing therapeutic coefficient. Studies have shown that alpha-helical polypeptide helicity enhanced antiviral polypeptides can improve the selectivity of the virus, i.e. the performance of the killing activity of the virus suppression and low toxicity for eukaryotic cells. alpha-helical anti-cancer peptides studies have shown that the helicity lower the lower the toxicity of red blood cells; helicity and anti-cancer activity of anti-cancer peptide between the optimum value, lower or higher than the optimal value will reduce its suppression of the killing effect of cancer. Suppression of the killing of the four bacteria helicity reduction can improve the antibacterial activity of antimicrobial peptides, but the reduction of the helicity best range, if reduced too much will make it inhibitory activity decreased even lose antibacterial capability.

Studies on the Effect of Heilicity of α-helical Peptides on Their Biological Activities

Abstract

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