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Gene Delivery for Intervertebral Disc
Published in Raquel M. Gonçalves, Mário Adolfo Barbosa, Gene and Cell Delivery for Intervertebral Disc Degeneration, 2018
Gianluca Vadalà, Luca Ambrosio, Vincenzo Denaro
Recently, Ellman et al. tested a combined peptide therapy using lactoferricin B (which was shown to exert anti-inflammatory, anticatabolic, and proanabolic effects on NP cells) and BMP-7 on bovine disc cells in vitro, demonstrating that the two factors together had a synergistic effect that resulted in higher aggrecan content when compared to the administration of a single factor alone (Ellman et al. 2013).
Synthesis of Bioactive Peptides for Pharmaceutical Applications
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Jaison Jeevanandam, Ashish Kumar Solanki, Shailza Sharma, Prabir Kumar Kulabhusan, Sapna Pahil, Michael K. Danquah
Recently, Pizzo et al. (2018) designed two antimicrobial peptides (IKY31 and IKY23) from the leaves of Phytolacca dioica and revealed their bacterial inhibition and anti-biofilm property against planktons and two strains of Gram-negative bacteria. Similarly, lactic acid bacteria that are naturally present in various fermented foods are the main bacteriocin peptide producers (Ahmed et al., 2017) and these peptides are commonly called antibiotics of endogenous origin due to their growth inhibition potential of several pathogenic microorganisms such as Bacillus cereus, Staphylococcus aureus Listeria monocytogenes, and Clostridium botulinum (Barbosa et al., 2017). There are numerous bacteriocins such as propionicin, nisin and diolococcin that are reported to be formed as a result of bacterial fermentation (Santos et al., 2018). Bioactive peptides are also extant in naturally occurring food products which include milk and dairy products. Milk-based biologically active peptides have elevated interest among researchers because they possess multifunctional properties that aid in modulating and triggering the immuno system simultaneously (Mohanty et al., 2016). Generally, the peptides are obtained from milk via proteolytic, fermentation and enzymatic methods. For instance, Aguilar-Toalá et al. (2017) obtained fractions of peptides and crude extracts (<3 and 3–10 kDa) from milk after fermentation using Lactobacillus plantarum bacterial strains and this showed that the crude milk extract possesses higher bioactivity than both peptide fractions with multifunctional properties such as higher anti-inflammatory, antihemolytic, and antioxidant activity. Multidrug resistance is the new route of bacterial pathogenicity towards their host which demands novel anti-bacterial agents. Thus, bioactive peptides derived from milk named as Lactoferrin (Lf) are employed to exhibit antimicrobial activities against bacteria, viruses and fungi by disrupting their cell membranes (Mohanty et al., 2016). Additionally, Vega et al. (2018) synthesized and screened three novel synthetic RRWQWR motif containing AMP based on lactoferricin B (LfcinB). These peptides exhibited a MIC50 value between 3.1–198 μM and a minimum bactericidal concentration (MBC) of 25–200 μM against healthcare associated infection causing pathogens. Caseicin is another milk-derived peptide with enhanced antimicrobial activity against C. sakazakii, S. aureus and S. Typhimurium, and are used as a coating over package material to protect powdered infant food products against microbial activity (Guinane et al., 2015). In the same way, Iglesias-Figueroa et al. (2016) produced recombinant bovine lactoferrin (rbLf) using Pichia pastoris, which displayed excellent bacterial growth inhibition properties against E. coli, S. aureus, and P. aeruginosa after subjected to pepsin digestion (Iglesias-Figueroa et al., 2016).
A bovine lactoferricin-lactoferrampin-encoding Lactobacillus reuteri CO21 regulates the intestinal mucosal immunity and enhances the protection of piglets against enterotoxigenic Escherichia coli K88 challenge
Published in Gut Microbes, 2021
Weichun Xie, Liying Song, Xueying Wang, Yigang Xu, Zengsu Liu, Dongfang Zhao, Shubo Wang, Xiaolong Fan, Zhaorui Wang, Chong Gao, Xiaona Wang, Li Wang, Xinyuan Qiao, Han Zhou, Wen Cui, Yanping Jiang, Yijing Li, Lijie Tang
Antimicrobial peptides (AMPs) are short cationic molecules (12–50 aa) with amphipathic structures, and these molecules play essential roles in host defense against microbial infection.9 Bovine lactoferricin (Lfcin B) and lactoferrampin (Lfampin) are two antimicrobial peptides released by gastric pepsin cleavage of bovine lactoferrin (LF).10 Lfcin B consists of a positively charged looped peptide containing residues 17–41, Lfampin comprises residues 268–284 in the N1 domain of LF.11 Recent reports have suggested that the fusion of Lfcin B with Lfampin (LFCA) broadens their antimicrobial spectra in vitro.12,13 In addition to its antimicrobial activity, the chimera has also been reported to be involved in improving performance, immune function and intestinal mucosal morphology.14 The synthesis and purification of AMPs are costly and time-consuming.15Lactobacillus has been considered a good delivery vehicle to express AMPs for preserving the mucosal integrity, improving intestinal microbiota and ameliorating DSS-induced intestinal injury.16,17
Advances in the use of cell penetrating peptides for respiratory drug delivery
Published in Expert Opinion on Drug Delivery, 2020
Larissa Gomes dos Reis, Daniela Traini
Preparation of polyplexes between CPPs and DNA has been reported in different studies. Gomes dos Reis et al., (2018) showed that the presence of CPPs was essential for intracellular delivery of pDNA in two different lung epithelial cell lines (A549 and Calu-3 cell lines) [75]. Baoum and Berkland (2010) and Alhakamy et al. (2016) showed that condensation using calcium chloride in association with arginine-rich CPPs electrostatic complexation produced smaller and more stable complexes that led to greater transfection efficiencies in A549 lung cells [76,77]. Using the same technique, Ishiguro et al (2017) condensed a modified version of TAT and pDNA using calcium chloride and showed efficient in vitro gene expression, as well as efficient growth inhibition of lung cancer in carcinoma xenographs of mouse lungs using intratracheal and intravenous administrations [78]. Using a slightly different method, Liu et al., (2016) complexed pDNA with a peptide derived from bovine lactoferricin. Differently from the studies presented above, the authors pre-treated the cells with 113 mM calcium chloride instead of using this compound in the coprecipitation method. However, in a similar manner, gene expression was increased in A549 cells when calcium chloride was present from 40- to 80-fold gene expression using different pDNAs [79].
Tear film, contact lenses and tear biomarkers
Published in Clinical and Experimental Optometry, 2019
Further investigations were undertaken to examine whether lactoferrin could potentiate the activity of traditional antibiotics, and vancomycin was used as it is a cell‐wall active antibiotic and often the last antibiotic that can be used to treat β‐lactam‐resistant (for example methicillin‐resistant) staphylococci or enterococci. Lactoferrin was able to decrease the minimum bactericidal and inhibitory concentrations of vancomycin needed to kill biofilms of S. epidermidis.1999 Perhaps of even greater significance was our finding that lactoferrin could reduce the resistance of enterococci to vancomycin. At the concentrations of lactoferrin found in tears (approximately 2-mg/ml) the minimum inhibitory concentration of vancomycin of vancomycin‐resistant strains of Enterococcus faecalis and E. faecium were reduced by 16‐ and eight‐fold, respectively.2001 These investigations were followed by others examining whether a small peptide called lactoferricin that can be released from lactoferrin could synergise with other antimicrobials. There was very little evidence that lactoferricin could synergise with ciprofloxacin, ceftazidime or gentamicin when used with S. aureus strains, but the combinations were not antagonistic.2010 On the other hand, lactoferricin could synergise with ciprofloxacin and ceftazidime, but not gentamicin, to increase the sensitivity of P. aeruginosa isolates to these antimicrobials.2010