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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
Burns and their associated wounds are an important public health problem throughout the world. The conventional curative therapies for burn wounds have drawbacks of increasing antibiotic resistance to the common pathogenic bacteria such as S. aureus, A. baumannii, and P. aeruginosa. Thus, antimicrobial peptides with a broad activity spectrum are a capable alternative for surgical wound treatments, burns, and other skin infections. For instance, human AMP cathelicidin (LL-37) controls inflammation and promotes wound healing by stimulating fibroblasts and epidermal cells to form a granulation tissue and thus promoting angiogenesis. Likewise, synthetic peptide LLKKK18 conjugated with dextrins not only was effective in wound healing but also promoted angiogenesis in C57-BL/6 mice. Similarly, Pexiganan, which is a promising derivative of antimicrobial magainin peptide, is efficient against 200 bacteria of Gram-positive and Gram-negative strains. Various synthetic peptides, such as HB107, HB1345, PXL-150, Novispirin G10, IK8L, D2A21, and SHAP1, were also delivered in burn wounds as nano-emulsions, which showed potential antimicrobial property against P. aeruginosa in preclinical and clinical trials. Moreover, a synthetic peptide called SHAP-1 promoted wound healing at a very low concentration and is reported to be stable, even when high salt concentrations and proteases are present (Lee et al., 2014). Another synthetic peptide, Novispirin-G10, is reported to possess rapid bacterial inhibition ability in partial-thickness burn wounds that are infected by P. aeruginosa. Further, a novel antimicrobial peptide (A3-APO), as either a dimer or a monomer, was found effective against wounds and skin burn infections caused by multi-drug-resistant strains of Acinetobacter baumannii (Javia et al., 2018; Heinbockel et al., 2018).
Design, recombinant expression, and antibacterial activity of a novel hybrid magainin–thanatin antimicrobial peptide
Published in Preparative Biochemistry & Biotechnology, 2019
Lu Tian, Di Zhang, Peng Su, Yuan Wei, Zhongzhong Wang, Pan Xue Wang, Chun Ji Dai, Guo Li Gong
In this study, novel synthetic hybrid antimicrobial peptide MT were rationally designed from magainin and thanatin to optimize and improve the direct antimicrobial effect of antimicrobial peptides against a broad spectrum of bacterial species. The hybrid MT protein was expressed and purified, and its minimum concentrations against Staphylococcus aureus, Escherichia coli DH5α, and Bacillus subtilis were 16.5, 20, and 9 μM, respectively. The MT antimicrobial activity was higher than that of the parent peptides and its function would contribute to the development of antimicrobial peptides as substitutes for antibiotics.