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New Engineered Fusion Peptide With Dual Functionality: Antibacterial and Strong Binding to Hydroxyapatite Publisher



Fateme R1 ; Fatemeh G2 ; Sima S1, 3 ; Moshaverinia A4 ; Hasannia S2, 5
Authors
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Authors Affiliations
  1. 1. Department of Dental Biomaterials, School of Dentistry/Research Center for Science and Technology in Medicine, Tehran University of Medical Sciences, Tehran, Iran
  2. 2. Novateb Research Laboratory, Dental Equipment and Bio-Material Technology Incubation Center, Tehran, Iran
  3. 3. Dental Research Center, Dentistry Research Institute, Tehran University of Medical Sciences, Tehran, Iran
  4. 4. Division of Advanced Prosthodontics, Weintraub Center for Reconstructive Biotechnology and Division of Advanced Prosthodontics, School of Dentistry, University of California Los Angeles, Los Angeles, CA, United States
  5. 5. Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran

Source: International Journal of Peptide Research and Therapeutics Published:2020


Abstract

One of the main challenges in oral disease is prevention of bacterial infections considering antibiotic resistance as a result of frequent use of conventional antibiotics. A natural alternative to these chemical antibiotics is antimicrobial peptide (AMP). LL37, a helical and amphipathic peptide with 37 amino acid residues, is the only cathelicidin-derived form of AMPs in humans that has a broad spectrum of antimicrobial activity (Majewski et al. in Cent Eur J immunol 43(4):453–457, https://doi.org/10.5114/ceji.2018.81355, 2018). In this study a bi-functional fusion peptide was designed, which consisted of LL-37 peptide linked to a hydroxyapatite (HA) binding peptide through a GGGGS linker. The fusion peptide antimicrobial activity was assessed against both gram-positive and gram-negative bacteria by the microtiter plate method and minimum inhibitory concentrations of 250 µg/ml and 125 µg/ml were obtained for Streptococcus mutans and Escherichia coli, respectively. The binding affinity of the HABP-LL37 fusion peptide to HA-surfaces was confirmed by the peptide release test using the spectrometer method. The HABP-LL37 fusion peptide immobilization on HA surfaces was done using a simple soaking technique. It was shown that 100 mg of the HA polymer disk could load up to 278 μg (55.6%) of LL37-HABP. Evaluation of the cytotoxic properties of the designed fusion peptide before and after immobilization on HA polymer disks against C2C12 cells showed that immobilization resulted in the reduction of HABP-LL37 cytotoxicity. The use of this bi-functional peptide with HA-based biomaterial can result in the development of novel and safe antimicrobial bone substitutes to manage and reduce the complications of device infection. © 2019, Springer Nature B.V.
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