Histatin 5

Research use only, not for human use.

Histatin 5 inhibits the activity of the host matrix metalloproteinases MMP-2 and MMP-9 with IC50s of 0.57 and 0.25 μM, respectively. Histatin 5 is a human basic salivary peptide with strong fungicidal properties in vitro.

Histatin 5 inhibits the activity of the host matrix metalloproteinases MMP-2 and MMP-9 with IC50s of 0.57 and 0.25 μM, respectively. Histatin 5 is a human basic salivary peptide with strong fungicidal properties in vitro.(In Vitro):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 inhibits 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 (IC50, 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. 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 μM inhibits state 2 respiration.

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 inhibits 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 (IC50, 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. 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 μM inhibits state 2 respiration.

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Metabolic Enzyme/Protease

MMP

IC50: 0.57 μM (MMP-2), 0.25 μM (MMP-9)

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115966-68-2

3036.29

C133H195N51O33

>98% (HPLC)

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Sequence:Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr

(-20℃)

With Ice Pack

≥ 2 years