scholarly journals The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions

2021 ◽  
Author(s):  
Bee Ha Gan ◽  
Josephine Gaynord ◽  
Sam M. Rowe ◽  
Tomas Deingruber ◽  
David R. Spring
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties ◽  
Synthetic Chemistry ◽  
Future Directions

This review discusses the diversity of structure and physicochemical properties of antimicrobial peptides and their derivatives, various chemical synthetic strategies that have been applied in their development, and how this links to their activity.

scholarly journals Correction: The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions

2022 ◽  
Author(s):  
Bee Ha Gan ◽  
Josephine Gaynord ◽  
Sam M. Rowe ◽  
Tomas Deingruber ◽  
David R. Spring
Keyword(s):  
Antimicrobial Peptides ◽  
Synthetic Chemistry ◽  
Future Directions

Correction for ‘The multifaceted nature of antimicrobial peptides: current synthetic chemistry approaches and future directions’ by Bee Ha Gan et al., Chem. Soc. Rev., 2021, 50, 7820–7880, DOI: 10.1039/D0CS00729C.

scholarly journals Improved Carotenoid Processing with Sustainable Solvents Utilizing Z-Isomerization-Induced Alteration in Physicochemical Properties: A Review and Future Directions

Molecules ◽  
2019 ◽  
Vol 24 (11) ◽  
pp. 2149 ◽  
Author(s):  
Masaki Honda ◽  
Hakuto Kageyama ◽  
Takashi Hibino ◽  
Yelin Zhang ◽  
Wahyu Diono ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Antioxidant Capacity ◽  
Amorphous State ◽  
Functional Difference ◽  
Geometric Isomers ◽  
Processing Efficiency ◽  
Future Directions ◽  
Sustainable Solvents ◽  
Low Efficiency ◽  
Low Solubility

Carotenoids—natural fat-soluble pigments—have attracted considerable attention because of their potential to prevent of various diseases, such as cancer and arteriosclerosis, and their strong antioxidant capacity. They have many geometric isomers due to the presence of numerous conjugated double bonds in the molecule. However, in plants, most carotenoids are present in the all-E-configuration. (all-E)-Carotenoids are characterized by high crystallinity as well as low solubility in safe and sustainable solvents, such as ethanol and supercritical CO2 (SC-CO2). Thus, these properties result in the decreased efficiency of carotenoid processing, such as extraction and emulsification, using such sustainable solvents. On the other hand, Z-isomerization of carotenoids induces alteration in physicochemical properties, i.e., the solubility of carotenoids dramatically improves and they change from a “crystalline state” to an “oily (amorphous) state”. For example, the solubility in ethanol of lycopene Z-isomers is more than 4000 times higher than the all-E-isomer. Recently, improvement of carotenoid processing efficiency utilizing these changes has attracted attention. Namely, it is possible to markedly improve carotenoid processing using safe and sustainable solvents, which had previously been difficult to put into practical use due to the low efficiency. The objective of this paper is to review the effect of Z-isomerization on the physicochemical properties of carotenoids and its application to carotenoid processing, such as extraction, micronization, and emulsification, using sustainable solvents. Moreover, aspects of Z-isomerization methods for carotenoids and functional difference, such as bioavailability and antioxidant capacity, between isomers are also included in this review.

scholarly journals Mode-of-Action of Antimicrobial Peptides: Membrane Disruption vs. Intracellular Mechanisms

2020 ◽  
Vol 2 ◽  
Author(s):  
Aurélie H. Benfield ◽  
Sónia Troeira Henriques
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties ◽  
Broad Spectrum ◽  
Mode Of Action ◽  
Bacterial Pathogens ◽  
Model Membranes ◽  
Membrane Disruption ◽  
Attractive Alternative ◽  
Bacterial Cells

Antimicrobial peptides are an attractive alternative to traditional antibiotics, due to their physicochemical properties, activity toward a broad spectrum of bacteria, and mode-of-actions distinct from those used by current antibiotics. In general, antimicrobial peptides kill bacteria by either disrupting their membrane, or by entering inside bacterial cells to interact with intracellular components. Characterization of their mode-of-action is essential to improve their activity, avoid resistance in bacterial pathogens, and accelerate their use as therapeutics. Here we review experimental biophysical tools that can be employed with model membranes and bacterial cells to characterize the mode-of-action of antimicrobial peptides.

scholarly journals Microbial Reduction of Cholesterol to Coprostanol: An Old Concept and New Insights

Catalysts ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 167 ◽  
Author(s):  
Aicha Kriaa ◽  
Mélanie Bourgin ◽  
Héla Mkaouar ◽  
Amin Jablaoui ◽  
Nizar Akermi ◽  
...  
Keyword(s):  
Gut Microbiota ◽  
Physicochemical Properties ◽  
Metabolic Pathways ◽  
Cholesterol Metabolism ◽  
Microbial Reduction ◽  
Reaction Intermediates ◽  
Future Directions ◽  
Microbial Enzymes ◽  
Shed Light

The gut microbiota plays a key role in cholesterol metabolism, mainly through the reduction of cholesterol to coprostanol. The latter sterol exhibits distinct physicochemical properties linked to its limited absorption in the gut. Few bacteria were reported to reduce cholesterol into coprostanol. Three microbial pathways of coprostanol production were described based on the analysis of reaction intermediates. However, these metabolic pathways and their associated genes remain poorly studied. In this review, we shed light on the microbial metabolic pathways related to coprostanol synthesis. Moreover, we highlight current strategies and future directions to better characterize these microbial enzymes and pathways.

scholarly journals Correlation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: Predicting experimental toxicity

Peptides ◽  
2008 ◽  
Vol 29 (7) ◽  
pp. 1085-1093 ◽  
Author(s):  
Allison A. Langham ◽  
Himanshu Khandelia ◽  
Benjamin Schuster ◽  
Alan J. Waring ◽  
Robert I. Lehrer ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties

Altered Activity and Physicochemical Properties of Short Cationic Antimicrobial Peptides by Incorporation of Arginine Analogues

2009 ◽  
Vol 6 (3) ◽  
pp. 996-1005 ◽  
Author(s):  
Johan Svenson ◽  
Rasmus Karstad ◽  
Gøril E. Flaten ◽  
Bjørn-Olav Brandsdal ◽  
Martin Brandl ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties ◽  
Cationic Antimicrobial Peptides

scholarly journals The future directions of synthetic chemistry

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Qing Zhu ◽  
Chao Liu
Keyword(s):  
Sustainable Energy ◽  
Synthetic Chemistry ◽  
New Materials ◽  
Future Directions ◽  
The Future

Abstract After being developed over hundred years, synthetic chemistry has created numerous new molecules and new materials to support a better life welfare. Even so, many challenges still remain in synthetic chemistry, higher selectivity, higher efficiency, environmental benign and sustainable energy are never been so wistful before. Herein, several topics surrounded the ability improvement of synthesis and the application enhancement of synthesis will be briefly discussed.

scholarly journals Physicochemical Properties That Enhance Discriminative Antibacterial Activity of Short Dermaseptin Derivatives

2006 ◽  
Vol 50 (8) ◽  
pp. 2666-2672 ◽  
Author(s):  
Shahar Rotem ◽  
Inna Radzishevsky ◽  
Amram Mor
Keyword(s):  
Antimicrobial Peptides ◽  
Physicochemical Properties ◽  
Culture Media ◽  
Gram Negative Bacteria ◽  
Terminal Sequence ◽  
Binding Properties ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria ◽  
Cytoplasmic Membranes

ABSTRACT Antimicrobial peptides are widely believed to exert their effects by nonspecific mechanisms. We assessed the extent to which physicochemical properties can be exploited to promote discriminative activity by manipulating the N-terminal sequence of the 13-mer dermaseptin derivative K4-S4(1-13) (P). Inhibitory activity determined in culture media against 16 strains of bacteria showed that when its hydrophobicity and charge were changed, P became predominantly active against either gram-positive or gram-negative bacteria. Thus, conjugation of various aminoacyl-lysin moieties (e.g., aminohexyl-K-P) led to inactivity against gram-positive bacteria (MIC50 > 50 μM) but potent activity against gram-negative bacteria (MIC50, 6.2 μM). Conversely, conjugation of equivalent acyls to the substituted analog M4-S4(1-13) (e.g., hexyl-M4-P) led to inactivity against gram-negative bacteria (MIC50 > 50 μM) but potent activity against gram-positive bacteria (MIC50, 3.1 μM). Surface plasmon resonance experiments, used to investigate peptides' binding properties to lipopolysaccharide-containing idealized phospholipid membranes, suggest that although the acylated derivatives have increased lipophilic properties with parallel antibacterial behavior, hydrophobic derivatives are prevented from reaching the cytoplasmic membranes of gram-negative bacteria. Moreover, unlike modifications that enhanced the activity against gram-positive bacteria, which also enhanced hemolysis, we found that modifications that enhanced activity against gram-negative bacteria generally reduced hemolysis. Thus, compared with the clinically tested peptides MSI-78 and IB-367, the dermaseptin derivative aminohexyl-K-P performed similarly in terms of potency and bactericidal kinetics but was significantly more selective in terms of discrimination between bacteria and human erythrocytes. Overall, the data suggest that similar strategies maybe useful to derive potent and safe compounds from known antimicrobial peptides.

scholarly journals Prediction of Antibacterial Activity from Physicochemical Properties of Antimicrobial Peptides

PLoS ONE ◽  
2011 ◽  
Vol 6 (12) ◽  
pp. e28549 ◽  
Author(s):  
Manuel N. Melo ◽  
Rafael Ferre ◽  
Lídia Feliu ◽  
Eduard Bardají ◽  
Marta Planas ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Antimicrobial Peptides ◽  
Physicochemical Properties
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