Histatin 5 (TFA)
(Synonyms: 富组蛋白5三氟乙酸盐) 目录号 : GC36230Histatin 5 TFA 抑制宿主基质金属蛋白酶 MMP-2 和 MMP-9 活性,IC50s 分别为 0.57 和 0.25 μM。
Sample solution is provided at 25 µL, 10mM.
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Histatin 5 TFA inhibits the activity of the host matrix metalloproteinases MMP-2 and MMP-9 with IC50s of 0.57 and 0.25 μM, respectively. IC50: 0.57 μM (MMP-2), 0.25 μM (MMP-9)
Histatin 5 is a member of a family of low-molecular-weight salivary proteins secreted by parotid, submandibular, and sublingual glands. Using biotinylated gelatin as a substrate, Histatin 5 is found to inhibit the activity of the host matrix metalloproteinases MMP-2 and MMP-9 with IC50s of 0.57 and 0.25 μM, respectively. To localize the domain responsible for this inhibition, three peptides containing different regions of Histatin 5 are synthesized and tested as inhibitors of MMP-9. Peptides comprising residues 1 to 14 and residues 4 to 15 of Histatin 5 show much lower inhibitory activities (IC50s, 21.4 and 20.5 μM, respectively), while a peptide comprising residues 9 to 22 showed identical activity to Histatin 5 against MMP-9. Kinetic analysis of the inhibition of the Arg-gingipain reveals that Histatin 5 is a competitive inhibitor, affecting only the Km with a Ki of 15 μM [1]. Histatin 5 is an inhibitor of mitochondrial respiration.The human salivary antifungal peptide Histatin 5 is taken up by Candida albicans cells and associates intracellularly with mitochondria. Histatin 5 inhibits respiration of isolated C. albicans mitochondria as well as the respiration of intact blastoconidia in a dose and time-dependent manner. Histatin 5 at a concentration of 33 uM inhibits state 2 respiration[2].
[1]. Gusman H, et al. Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontaldisease. Infect Immun. 2001 Mar;69(3):1402-8. [2]. Helmerhorst EJ, et al. The human salivary peptide histatin 5 exerts its antifungal activity through the formation ofreactive oxygen species. Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14637-42.
Cas No. | SDF | ||
别名 | 富组蛋白5三氟乙酸盐 | ||
分子式 | C135H196N51F3O35 | 分子量 | 3150.31 |
溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
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1 mg | 5 mg | 10 mg | |
1 mM | 0.3174 mL | 1.5871 mL | 3.1743 mL |
5 mM | 0.0635 mL | 0.3174 mL | 0.6349 mL |
10 mM | 0.0317 mL | 0.1587 mL | 0.3174 mL |
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Human salivary peptides derived from histatins
Eur J Morphol 2003 Apr;41(2):99-102.PMID:15621863DOI:10.1080/09243860412331282200.
Human saliva from a healthy donor was subjected to fractionation by gel chromatography and six pools were collected and analysed by MALDI-TOF-MS and HPLC-ESI-MS. Three peptides, corresponding to 888.3, 687.3, and 524.1 amu and SNYLYDN, YLYDN, and LYDN sequences (determined by automated Edman sequencing), were isolated from pool 4. YLYDN was not previously described in human saliva. The peptides show the common C-terminal sequence of histatin 3 and histatin 1. To exclude the possibility that the three peptides were an artifact of the purification procedure, nine samples of human saliva were collected from healthy donors, immediately acidified with 0.2% TFA, and analysed by RP-HPLC-ESI-MS. The three peptides were detected in all the analyzed samples. SNYLYDN was always found at a concentration higher than that of YLYDN and LYDN. A correlation analysis performed on quantitative data indicated that the three peptides derive only from histatin 3. Other already known histatins also were searched for in the chromatogram. Histatins 1, 2, 3, 5, 6, 7, 8, and 10 were observed, although not in all samples analyzed, whereas other minor histatins were not detected.
Analysis of salivary peptides using HPLC-electrospray mass spectrometry
Biomed Chromatogr 2004 Oct;18(8):570-5.PMID:15386514DOI:10.1002/bmc.358.
Salivary peptides are involved in a wide range of functions constituting the first line of defence of oral cavity and precursors of dental pellicle formation. The presence of mucins in saliva makes difficult the analysis of the proteic content. This is due mainly to aggregation phenomenon between mucins and other high molecular weight glycoproteins and salivary proteins. Considering the importance of salivary peptides in biological functions, we have evaluated the influence of four different extraction methodologies on the separation and identification of these proteins by HPLC-MS. Based on their molecular weight, we identified a total of 22 peptides when extraction was performed using a solution of guanidine (6 m), compared with 14 peptides identified when saliva is acidified with TFA, which is an often used procedure. Our results also show the presence of mucin bind peptides, which include statherin, PRP1, PRP3, Histatin 1 and Histatin 5.