Effects of histatin-derived peptides immobilization by tresyl chloride-activation technique for MC3T3-E1 cellular responses on titanium (Ti) were evaluated. MC3T3-E1 were cultured on sandblasted and acid-etched Ti disks immobilized with histatin-derived peptides, including histatin-1, JH8194, and mixed histatin-1 with JH8194. Surface topography and cellular morphology were examined using a scanning electron microscope. Elemental composition and conformational peptides on Ti surface were examined using energy dispersive X-ray and fourier transform infrared spectroscopy, respectively. Cellular adhesion, proliferation, osteogenesis-related genes, and alkaline phosphatase activity were evaluated. The results showed that peptides were successfully immobilized on Ti surface. Cell attachments on histatin-1 and mixed peptides coated groups are higher than control. Histatin-1 achieved the significantly highest cellular proliferation. Histatin-derived peptides improved the osteogenesis related-gene expression and alkaline phosphatase activity (p<0.05). This study suggested that histatin-1 immobilization by tresyl chloride-activation technique enhanced cellular responses and might be able to promote cellular activities around the dental implants.
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http://dx.doi.org/10.4012/dmj.2020-307 | DOI Listing |
Effects of histatin-derived peptides immobilization by tresyl chloride-activation technique for MC3T3-E1 cellular responses on titanium (Ti) were evaluated. MC3T3-E1 were cultured on sandblasted and acid-etched Ti disks immobilized with histatin-derived peptides, including histatin-1, JH8194, and mixed histatin-1 with JH8194. Surface topography and cellular morphology were examined using a scanning electron microscope.
View Article and Find Full Text PDFQ Rev Biophys
March 2020
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, H-1117, Hungary.
Here it is demonstrated how some anionic food additives commonly used in our diet, such as tartrazine (TZ), bind to DHVAR4, an antimicrobial peptide (AMP) derived from oral host defense peptides, resulting in significantly fostered toxic activity against both Gram-positive and Gram-negative bacteria, but not against mammalian cells. Biophysical studies on the DHVAR4-TZ interaction indicate that initially large, positively charged aggregates are formed, but in the presence of lipid bilayers, they rather associate with the membrane surface. In contrast to synergistic effects observed for mixed antibacterial compounds, this is a principally different mechanism, where TZ directly acts on the membrane-associated AMP promoting its biologically active helical conformation.
View Article and Find Full Text PDFOral Dis
November 2013
Department of Periodontology and Oral Biology, Henry M. Goldman School of Dental Medicine, Boston, MA, USA.
Periodontal disease is characterised by proteolytic processes involving enzymes that are released by host immune cells and periodontal bacteria. These enzymes, when detectable in whole saliva, may serve as valuable diagnostic markers for disease states and progression. Because the substrate specificities of salivary proteases in periodontal health and disease are poorly characterised, we probed these activities using several relevant substrates: (i) gelatin and collagen type IV; (ii) the Arg/Lys-rich human salivary substrate histatin-5; and (iii) a histatin-derived synthetic analog benzyloxycarbonyl-Arg-Gly-Tyr-Arg-methyl cumaryl amide (Z-RGYR-MCA).
View Article and Find Full Text PDFAntimicrob Agents Chemother
September 2007
Section Nuclear Medicine, Division of Radiology, Leiden University Medical Center, Room C4-R-77, Albinusdreef 2, 2333 ZA Leiden, The Netherlands.
Homodimerization of histatin-derived peptides generally led to improved bactericidal activity against Staphylococcus aureus in vitro. In vivo, monomers and dimers were equally active in killing bacteria in mice with a soft tissue infection. Altogether, these peptides are promising compounds for the development of novel therapeutics against infections with drug-resistant bacteria.
View Article and Find Full Text PDFExpert Opin Emerg Drugs
May 2002
Demegen, Inc., 313 Pleasant Street, Watertown, MA 02472, USA.
Histatins are a family of histidine-rich, cationic peptides composed of up to 38 amino acids. They are secreted by the salivary glands of humans and some subhuman primates and are thought to be part of the host defence system in the oral cavity. Histatins exhibit in vitro activity against both bacteria and yeast, common to other antimicrobial peptides.
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