Peptides containing d -amino acids and retro-inverso peptides

Cardoso, Marlon Henrique; Cândido, Elizabete de Souza; Oshiro, Karen G. N.; Rezende, Samilla B.; Franco, Octávio L.

doi:10.1016/b978-0-08-100736-5.00005-3

Cited by 18 publications

(6 citation statements)

References 80 publications

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“…Simply replacing l -amino acids with d -amino acids, however, is generally ineffective as the side-chain orientation is completely altered with respect to the target . To guarantee structural stability, spatial orientation, side-chain topology, and overall peptide bioactivity, an alternative strategy is to engineer retro-derivatives, which can be built by reversing the d -peptide sequence while flipping its termini, thus restoring the l -amino side chain angles. ,, Retro-inverso variants are known to present high topochemical similarities with their precursors and preserve bioactivities.…”

Section: Results and Discussionmentioning

confidence: 99%

Synthetic Antibiotic Derived from Sequences Encrypted in a Protein from Human Plasma

et al. 2022

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Encrypted peptides have been recently found in the human proteome and represent a potential class of antibiotics. Here we report three peptides derived from the human apolipoprotein B (residues 887−922) that exhibited potent antimicrobial activity against drug-resistant Klebsiella pneumoniae, Acinetobacter baumannii, and Staphylococci both in vitro and in an animal model. The peptides had excellent cytotoxicity profiles, targeted bacteria by depolarizing and permeabilizing their cytoplasmic membrane, inhibited biofilms, and displayed anti-inflammatory properties. Importantly, the peptides, when used in combination, potentiated the activity of conventional antibiotics against bacteria and did not select for bacterial resistance. To ensure translatability of these molecules, a protease resistant retro-inverso variant of the lead encrypted peptide was synthesized and demonstrated anti-infective activity in a preclinical mouse model. Our results provide a link between human plasma and innate immunity and point to the blood as a source of much-needed antimicrobials.

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Section: Results and Discussionmentioning

confidence: 99%

Synthetic Antibiotic Derived from Sequences Encrypted in a Protein from Human Plasma

et al. 2022

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“…Among the challenges involved in developing AMPs for clinical applications we can mention: (i) the divergence between in vitro and in vivo antibacterial assays in terms of biological complexity, thus compromising accurate prediction of antiinfectious potential in AMPs at clinical level (Bjorn et al, 2012;Maiti et al, 2014); (ii) AMP susceptibility to enzymatic degradation, thus compromising the bioavailability of these antimicrobials, which represents an obstacle for oral/intravenous administration (Vlieghe et al, 2010;Cardoso et al, 2018b); and (iii) cost of synthesis compared with other small molecule drugs (Bray, 2003).…”

Section: Conclusion -Are We Generating Effective Drug Candidates?mentioning

confidence: 99%

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

et al. 2020

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Computer-Aided Design of Antimicrobial Peptides http://crdd.osdd.net/raghava/antibp2/ ClassAMP Uses RF and SVM to predict the propensity of a protein sequence to have antibacterial, antifungal, or antiviral activity http://www.bicnirrh.res.in/classamp/ AMPA Web tool for assessing the antimicrobial domains of proteins, with a focus on the design on new antimicrobial drugs http://tcoffee.crg.cat/apps/ampa/do DBAASP Provides users with information on detailed structure (chemical, 3D) and activity for those peptides, for which antimicrobial activity against particular target species have been evaluated experimentally https://dbaasp.org/home Joker An algorithm to design antimicrobial peptides using their language https://github.com/williamfp7/Joker

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“…For RSV, the phosphoprotein N-terminus (P 1-40) binds to a large cavity of N 0 , impairing N oligomerization. More specifically, NMR and biochemical studies have suggested that P (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) of RSV folds into an alpha helix upon binding to N 0 [11] (Fig. 3B).…”

Section: Targeting Conserved Viral Fusion and Replication Mechanisms ...mentioning

confidence: 99%

“…Stability after incubation with lysosome is increased in the range from hours to weeks depending on length of d-amino acid retroinverso stretches. [16]…”

Section: Peptidomimetics Applied To Antimicrobialsmentioning

confidence: 99%

Peptide Technologies at Energypolis

Mathieu

Nyanguile

2021

Chimia

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The new Energypolis campus brings together the skills of EPFL Valais-Wallis, HES-SO Valais-Wallis, and the Ark Foundation's services. Together these partners respond to today's major concerns in the domains of energy, health, and the environment cutting-edge technology. The spirit of this new campus is to foster innovation in these disciplines and emulate the creation of start-up companies. The HES-SO hosts the School of Engineering (HEI) at this campus, which includes the following degree programmes: Life Technologies, Systems Engineering and Energy and Environmental Engineering, as well as their corresponding applied research institutes. Peptide technologies belong to the many activities that are carrying out in the Institute of Life Technologies. The present review summarizes the peptide technologies that are currently under development, that is, the regioselective labeling of therapeutic antibodies for cancer imaging, the development of peptide antivirals and antimicrobials for the treatment of infectious diseases, targeting of drugs conjugated to peptidic scaffolds as well as engineering of biomaterials.

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Peptides containing d -amino acids and retro-inverso peptides

Cited by 18 publications

References 80 publications

Synthetic Antibiotic Derived from Sequences Encrypted in a Protein from Human Plasma

Synthetic Antibiotic Derived from Sequences Encrypted in a Protein from Human Plasma

Computer-Aided Design of Antimicrobial Peptides: Are We Generating Effective Drug Candidates?

Peptide Technologies at Energypolis

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