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Nanotechnology and Delivery System for Bioactive Antibiofilm Dental Materials
Published in Mary Anne S. Melo, Designing Bioactive Polymeric Materials for Restorative Dentistry, 2020
Jin Xiao, Yuan Liu, Marlise I. Klein, Anna Nikikova, Yanfang Ren
Meanwhile, C16G2 rinse usage was associated with reductions in plaque and salivary S. mutans, lactic acid production, and enamel demineralization (Sullivan et al. 2011). However, the high cost of producing sufficient amounts of AMPs usually is a major barrier to their clinical development and commercialization. Liu, Kamesh et al. (2016) developed an exciting low-cost approach using plant-made AMPs protegrin with complex secondary structures for topical use to control biofilms. The plant-made protegrin rapidly killed the pathogen S. mutans and impaired biofilm formation following a single topical application of the tooth-mimetic surface. Furthermore, a synergistic approach using AMPs combined with matrix-degrading enzymes can facilitate the peptide’s access into biofilms and kill the embedded bacteria (Liu, Kamesh, et al. 2016).
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
The dependency of peptide backbone chirality on cellular uptake has also been explored, with studies indicating that some CPPs, like penetratin and SynB (a protegrin-derived peptide), are able to penetrate the cellular membrane independently of its chirality [33,37,38]. However, Drin et al. [38] indicated higher retention of D-stereoisomer, which was associated with greater resistance of this stereoisomer to proteolysis. Verdurmen et al. [39] showed in their study using penetratin, a direct penetration mechanism occurs, in which two steps are necessary for the uptake: a heparan sulfate (HS)-binding step, followed by a membrane translocation step. The authors showed that although D- and L-stereoisomers had similar binding affinities with HS, L-CPPs were taken up more efficiently, indicating higher translocation for the L-stereoisomer [39]. Similarly, Najjar et al. [40] showed a longer effect for the D-amino acid in comparison to the L-amino acid counterpart, as the D-stereoisomer had a higher protease resistance without affecting the cellular uptake pathway [40].
Human antimicrobial peptides in autoimmunity
Published in Autoimmunity, 2020
Ekaterina S. Umnyakova, Maria S. Zharkova, Mikhail N. Berlov, Olga V. Shamova, Vladimir N. Kokryakov
Alexander Panyutich with his group started the investigations that revealed protein-protein interactions of several β-structural AMPs with C1 complex: human α-defensin-1 (HNP-1), porcine cathelicidin protegrin-1 and antimicrobial peptide from horseshoe crab Tachypleus tridentatus – tachyplesin-1 [55]. According to the cited work, proteins of C1 complex like serine proteinases C1r and C1s as well as serpin C1inh participated in AMPs binding, but not the C1q protein. Later by other authors, it was shown that HNP-1 and tachyplesin-1 form complexes with C1q directly [56,57,138,143]. The results of our investigations [144] showed that protegrin-1 interacts with C1q directly, as well as another peptide, arenicin-1 from the lugworm Arenicola marina [145]. Without any doubts, described phenomena affect the complement activation.
Murepavadin: a new antibiotic class in the pipeline
Published in Expert Review of Anti-infective Therapy, 2018
Ignacio Martin-Loeches, Glenn E. Dale, Antoni Torres
The outer membrane of gram-negative bacteria consisting mainly of lipopolysaccharides (LPS) and outer-membrane proteins (OMPs) is in principle attractive for developing new gram-negative bacteria-specific antibiotics [33,34]. Naturally occurring peptides and proteins make interesting starting points for the design and synthesis of biologically active peptidomimetics. By applying the protein epitope mimetic (PEM) approach, β-hairpin molecules based upon a series of β-hairpin-shaped host defense peptides, such as protegrin I (PG-1), libraries of macrocyclic PEM molecules based on a 14-residue PEM-scaffold were synthesized and screened for antibacterial activity [33,35,36]. Murepavadin (formally known as POL7080; Figure 1) is an antimicrobial peptidomimetic with a novel, nonlytic mechanism of action, first in class of Outer Membrane Protein Targeting Antibiotics (OMPTA) which is being developed by Polyphor Ltd [37,38]. The OMPTA molecules are fully synthetic and can be made in essentially 4 steps. The molecules contain loop sequences related to PG-1, but template-stabilized by a D-proline-L-proline sequence which helps to stabilize the β-hairpin conformation which is critical for the antibacterial activity [39]. One such peptide L8-1 had antimicrobial activity like that of PG-1 but with reduced hemolytic activity on human red blood cells [35]. Further optimization resulted in the discovery of a series of macrocyclic peptides which are nonhemolytic with Pseudomonas-specific activity, which finally led to the discovery of Murepavadin [38].