Basic peptide protamine exerts antimicrobial activity against periodontopathic bacteria——Growth inhibition of periodontopathic bacteria by protamine
Tadashi Miura, Keishi Iohara, Tetsuo Kato, Kazuyuki Ishihara, Masao Yoshinari
DOI: 10.4236/jbise.2010.311138   PDF    HTML     5,917 Downloads   11,156 Views   Citations


Protamine was investigated for its antibacterial activity against the periodontal pathogens, Porphyromonas gingivalis, Prevotella intermedia and Aggregatibacter actinomycetemcomitans. We determined the minimum inhibitory concentrations of protamine and its hydrolysate and their bactericidal activity. Protamine inhibited the growth of all periodontopathic bacteria tested on agar plates. Protamine, which MIC was 6.3 × 10-7 g L-1, was most effective against P. gingivalis. The antibacterial effect of native protamine was higher than that of its hydrolysate. An ATP bioluminescence assay revealed that protamine showed bactericidal activity against P. gingivalis in a time-dependent manner. These results indicate that protamine could be candidate peptide for prevention of P. gingivalis infection.

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Miura, T. , Iohara, K. , Kato, T. , Ishihara, K. and Yoshinari, M. (2010) Basic peptide protamine exerts antimicrobial activity against periodontopathic bacteria——Growth inhibition of periodontopathic bacteria by protamine. Journal of Biomedical Science and Engineering, 3, 1069-1072. doi: 10.4236/jbise.2010.311138.

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The authors declare no conflicts of interest.


[1] Sumida, S., Ishihara, K., Kishi, M. and Okuda, K. (2002) Transmission of periodontal disease-associated bacteria from teeth to osseointegrated implant regions. International Journal of Oral & Maxillofacial Implants, 17(5), 696-702.
[2] Slots, J. and Genco, R.J. (1984) Black-pigmented Bacteroides species, Capnocytophaga species, and Actinobacillus actinomycetemcomitans in human periodontal disease: Virulence factors in colonization, survival, and tissue destruction. Journal of Dental Research, 63(3), 412- 421.
[3] Dzink, J.L., Tanner, A.C., Haffajee, A.D., Socransky, S.S. (1985) Gram negative species associated with active destructive periodontal lesions. Journal of Clinical Periodontology, 12(8), 648-659.
[4] Sweeney, E.A., Alcoforado, G.A., Nyman, S. and Slots, J. (1987) Prevalence and microbiology of localized prepubertal periodontitis. Oral Microbiology and Immunology, 2(2), 65-70.
[5] Yoshinari, M., Oda, Y., Kato, T. and Okuda, K. (2001) Influence of surface modifications to titanium on antibacterial activity in vitro. Biomaterials, 22(14), 2043- 2048
[6] Norowski, P.A. Jr. and Bumgardner, J.D. (2009) Biomaterial and antibiotic strategies for peri-implantitis: A review. Journal of Biomedical Materials Research Part B: Applied Biomaterials, 88(2), 530-543.
[7] Yoshinari, M., Kato, T., Matsuzaka, K., Hayakawa, T. and Shiba, K. (2010) Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides. Biofouling, 26(1), 103-110.
[8] Yoshinari, M., Kato, T., Matsuzaka, K., Hayakawa, T., Inoue, T., Oda, Y., Okuda, K. and Shimono, M. (2006) Adsorption behavior of antimicrobial peptide histatin 5 on PMMA. Journal of Biomedical Materials Research Part B: Applied Biomaterials, 77(1), 47-54.
[9] Evans, E.W., Beach, F.G., Moore, K.M., Jackwood, M.W., Glisson, J.R. and Harmon, B.G. (1995) Antimicrobial activity of chicken and turkey heterophil peptides CHP1, CHP2, THP1, and THP3. Veterinary Microbiology, 47(3-4), 295-303.
[10] Roque, A., Orrego, M., Ponte, I. and Suau, P. (2004) The preferential binding of histone H1 to DNA scaffold-asso- ciated regions is determined by its C-terminal domain. Nucleic Acids Research, 32(20), 6111-6119.
[11] Li, Y.T., Kwon, Y.M., Spangrude, G.J., Liang, J.F., Chung, H.S., Park, Y.J. and Yang, V.C. (2009) Preliminary in vivo evaluation of the protein transduction domain- modified ATTEMPTS approach in enhancing asparaginase therapy. Journal of Biomedical Materials Research Part A, 91(1), 209-220.
[12] Sarwar, G., Kakimoto, D., Onishi, M. and Nagata, R. (1989) Potentiality of protamine sulfate as mutagen. Journal of Toxicological Sciences, 14(3), 215-225.
[13] Tsukiyama, R., Katsura, H., Tokuriki, N. and Kobayashi, M. (2002) Antibacterial activity of licochalcone A against spore-forming bacteria. Antimicrob Agents Chemother, 46(5), 1226-1230.
[14] Agren, G. (1954) Investigations of substances inhibiting or stimulating the growth of some lactobacilli. III. Effects of protamin and some heat-stable protein fractions from spleen and urine. Acta Pathologica Microbiologica Scandinavica, 35(1), 97-104.
[15] Burton, E., Gawande, P.V., Yakandawala, N., LoVetri, K., Zhanel, G.G., Romeo, T., Friesen, A.D. and Madhyastha, S. (2006) Antibiofilm activity of GlmU enzyme inhibitors against catheter-associated uropathogens. Antimicrob Agents Chemother, 50(5), 1835-1840.
[16] Miura, T., Hayakawa, T., Okumori, N., Iohara, K. and Yoshinari, M. (2010) Antifungal activity against Candida albicans on PMMA coated with protamine derivatives. Journal of Oral Tissue Engineering, in Press.
[17] Hoffmann, J.A., Chance, R.E. and Johnson, M.G. (1990) Purification and analysis of the major components of chum salmon protamine contained in insulin formulations using high-performance liquid chromatography. Protein Expression and Purification, 1(2), 127-133.
[18] Hunter, R.G., Henry, G.W. and Heinicke, R.M. (1957) The action of papain and bromelain on the uterus. American Journal of Obstetrics and Gynecology, 73(4), 867-874.

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