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Purification, Characterazation and Biological Activity of Bioactive Peptides from the Skin of Rana Chensinensis

Author: LiJunFeng
Tutor: ShangDeJing
School: Liaoning Normal University
Course: Cell Biology
Keywords: Chinese forest frog Skin Bioactive peptides Separation and purification Structural identification Mass spectrometric detection
CLC: Q51
Type: Master's thesis
Year: 2009
Downloads: 222
Quote: 2
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Abstract


Amphibians evolved from aquatic fish to the transition between the groups in the real terrestrial reptiles, their skin maintain amphibians survive and adapt to the habitat of diverse ecological environment plays an important role, its survival must respiration, regulating water, against predation, anti-microbial invasion, excretion and reproductive functions. Amphibian skin is a good source of bioactive peptides, its content is much more than the content derived from mammalian various organizations analogues. Because the skin of the different species in the presence of different types of bioactive molecules, so the biologically active polypeptide has a molecular and functional diversity unimaginable. The skin of amphibians is a very easy access to the resources, suitable for the discovery of bioactive peptides, purification and functional studies. Rana (Rana CHENSINENSIS) is an important economic frogs, but also the Northeast regional advantages medicinal value of animal resources one. Studies have shown that frog skin is a rich source of the active peptides resources their skin glands contain a variety of active factor, including moisturizing factor, polypeptide growth factors, of Rana biological antibacterial factor, angiotensin factor, bombesin factor bradykinin-like polypeptide, thyrotropin peptides, morphine factor on 14 peptide factor. If you focus on disease treatment drug screening and discovery of biologically active molecules, the important value of Chinese forest frog skin Acquisition and structural analysis of bioactive peptides, will be able to enrich the Beijing Pharmaceutical resources for more effective development Rana resources to lay a solid foundation. The paper select the Benxi mountain foot at the end of the Changbai Mountain Rana as experimental material, the use of gel chromatography and reverse-phase high performance liquid chromatographic techniques to extract the skin bio-active peptides, separation and purification, and purification methods and conditions filter optimization, six kinds of skin bioactive peptides. MS and Q-TOF MS / MS six kinds of the molecular weight of the polypeptide and the amino acid Ordering sequence were determined. First, induced by electrical stimulation of the skin secretion of Rana liquid. Using ShephadexG50 gel chromatography and VydacTP510 reversed-phase high performance liquid chromatography combined use means using a linear gradient elution six purified peptides from the skin secretion of fluid. The amino acid sequence analysis showed that three of the six peptides bradykinin bradykinin peptide-related peptide, three antimicrobial peptides, from 1059.63 to 3285.96 Dalton molecular weight by 9-27 amino acids. Its primary structure were the RPPGFSPFR, RPPGFSPFRAL, RPPGFSSEDRPSAP, MHDEHACTGD, KMDLLKV AVNKLLAAHHRHC LLDGLL and KFWVKRLKRGKNVARTLKEIKLFSTPT. NCBI protein database than right, polypeptide RPPGFSPFR is the 9 amino acids of the typical bradykinin (bradykinin); the structural domain conserved sequence RPPGFS of the polypeptide RPPG FSPFRAL RPPGFSSEDRPSAP bradykinin, belonging to bradykinin-related peptide BRPs (bradykinin -Related Peptides). In the database, the polypeptide MHDEHACTG, KMDLLKVAVNKLLAAHHRHCLLDGLL KFWVKRLKRGKNVARTLKEIKLFSTPT with low similarity to other amphibian skin peptides are known to belong to the new peptide. These six polypeptides were named Bradykinin-RC-RC1 Ranakinin Ranakinin-RC2, Chensinin-2, Chensinin-3 and Chensinin-4. Antibacterial activity analysis showed that the Chinese forest frog skin small molecule active peptides have strong antibacterial activity, which Chensinin-3, Chensinin-4 with broad-spectrum antimicrobial activity against Gram-positive bacteria and gram-negative bacteria has inhibition of bradykinin-RC inhibit Staphylococcus aureus. Isolated guinea pig ileum assay 3 bradykinin and bradykinin-related peptide on intestinal muscle. Experimental results show that the bradykinin-RC and Ranakinin of-RC1 can make guinea pig ileum muscle contraction significantly, and the contraction strength and peptide concentrations are positively correlated Ranakinin-RC1 bradykinin activity than typical bradykinin the peptide BRADYKININ-RC contraction activity . Ranakinin-RC2 not bradykinin activity.

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CLC: > Biological Sciences > Biochemistry > Protein
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