Stimuli-responsive conformational transformation of antimicrobial peptides stapled with an azobenzene unit

2020 ◽  
Vol 44 (35) ◽  
pp. 14777-14780
Author(s):  
Jeonghun Lee ◽  
Hanwool Lee ◽  
Chulhee Kim
Keyword(s):  
Antimicrobial Peptides ◽  
Uv Irradiation ◽  
Reductive Cleavage ◽  
Helical Conformation ◽  
Conformational Transformation ◽  
Stimuli Responsive

The effect of the azobenzene-stapling position on the triggered transformation of the helical conformation of KLA peptides in response to UV irradiation and reductive cleavage is investigated.

Solution structures of stomoxyn and spinigerin, two insect antimicrobial peptides with an α-helical conformation

Biopolymers ◽  
2006 ◽  
Vol 81 (2) ◽  
pp. 92-103 ◽  
Author(s):  
Céline Landon ◽  
Hervé Meudal ◽  
Nathalie Boulanger ◽  
Philippe Bulet ◽  
Françoise Vovelle
Keyword(s):  
Antimicrobial Peptides ◽  
Helical Conformation ◽  
Solution Structures

scholarly journals pH- and concentration-dependent supramolecular self-assembly of a naturally occurring octapeptide

2020 ◽  
Vol 16 ◽  
pp. 2017-2025
Author(s):  
Goutam Ghosh ◽  
Gustavo Fernández
Keyword(s):  
Self Assembly ◽  
Ph Value ◽  
Secondary Structures ◽  
Random Coil ◽  
Conformational Transformation ◽  
Stimuli Responsive ◽  
Responsive Materials ◽  
Force Microscopy ◽  
Assembly Behavior ◽  
Novel Drug

Peptide-based biopolymers represent highly promising biocompatible materials with multiple applications, such as tailored drug delivery, tissue engineering and regeneration, and as stimuli-responsive materials. Herein, we report the pH- and concentration-dependent self-assembly and conformational transformation of the newly synthesized octapeptide PEP-1. At pH 7.4, PEP-1 forms β-sheet-rich secondary structures into fractal-like morphologies, as verified by circular dichroism (CD), Fourier-transform infrared (FTIR) spectroscopy, thioflavin T (ThT) fluorescence spectroscopy assay, and atomic force microscopy (AFM). Upon changing the pH value (using pH 5.5 and 13.0), PEP-1 forms different types of secondary structures and resulting morphologies due to electrostatic repulsion between charged amino acids. PEP-1 can also form helical or random-coil secondary structures at a relatively low concentration. The obtained pH-sensitive self-assembly behavior of the target octapeptide is expected to contribute to the development of novel drug nanocarrier assemblies.

Linking sequence patterns and functionality of alpha-helical antimicrobial peptides

2018 ◽  
Vol 35 (16) ◽  
pp. 2713-2717 ◽  
Author(s):  
Igor E Eliseev ◽  
Ivan N Terterov ◽  
Anna N Yudenko ◽  
Olga V Shamova
Keyword(s):  
Antimicrobial Peptides ◽  
Rational Design ◽  
Therapeutic Potential ◽  
Deep Understanding ◽  
Supplementary Information ◽  
Helical Conformation ◽  
Efficient Design ◽  
Sequence Patterns ◽  
Functional Features ◽  
Natural Peptides

Abstract Motivation The rational design of antimicrobial peptides (AMPs) with increased therapeutic potential requires deep understanding of the determinants of their activities. Inspired by the computational linguistic approach, we hypothesized that sequence patterns may encode the functional features of AMPs. Results We found that α-helical and β-sheet peptides have non-intersecting pattern sets and therefore constructed new sequence templates using only helical patterns. Designed peptides adopted an α-helical conformation upon binding to lipids, confirming that the method captures structural and biophysical properties. In the antimicrobial assay, 5 of 7 designed peptides exhibited activity against Gram(+) and Gram(–) bacteria, with most potent candidate comparable to best natural peptides. We thus conclude that sequence patterns comprise the structural and functional features of α-helical AMPs and guide their efficient design. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals Antimicrobial Activities and Structures of Two Linear Cationic Peptide Families with Various Amphipathic β-Sheet and α-Helical Potentials

2005 ◽  
Vol 49 (12) ◽  
pp. 4957-4964 ◽  
Author(s):  
Yi Jin ◽  
Janet Hammer ◽  
Michelle Pate ◽  
Yu Zhang ◽  
Fang Zhu ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Plasma Membranes ◽  
Membrane Lipids ◽  
Lipid Vesicles ◽  
Selective Advantage ◽  
Antimicrobial Activities ◽  
Helical Conformation ◽  
Bacterial Cells ◽  
Β Sheet

ABSTRACT Many naturally occurring antimicrobial peptides comprise cationic linear sequences with the potential to adopt an amphipathic α-helical conformation. We designed a linear 18-residue peptide that adopted an amphipathic β-sheet structure when it was bound to lipids. In comparison to a 21-residue amphipathic α-helical peptide of equal charge and hydrophobicity, this peptide possessed more similar antimicrobial activity and greater selectivity in binding to and inducing leakage in vesicles composed of bacterial membrane lipids than vesicles composed of mammalian membrane lipids (J. Blazyk, R. Weigand, J. Klein, J. Hammer, R. M. Epand, R. F. Epand, W. L. Maloy, and U. P. Kari, J. Biol. Chem. 276:27899-27906, 2001). Here, we compare two systematically designed families of linear cationic peptides to evaluate the importance of amphipathicity for determination of antimicrobial activity. Each peptide contains six lysine residues and is amidated at the carboxyl terminus. The first family consists of five peptides with various capacities to form amphipathic β-sheet structures. The second family consists of six peptides with various potentials to form amphipathic α helices. Only those peptides that can form a highly amphipathic structure (either a β sheet or an α helix) possessed significant antimicrobial activities. Striking differences in the abilities to bind to and induce leakage in membranes and lipid vesicles were observed for the two families. Overall, the amphipathic β-sheet peptides are less lytic than their amphipathic α-helical counterparts, particularly toward membranes containing phosphatidylcholine, a lipid commonly found in mammalian plasma membranes. Thus, it appears that antimicrobial peptides that can form an amphipathic β-sheet conformation may offer a selective advantage in targeting bacterial cells.

Specific HER2 targeting and triggered drug release by conformational transformation of a dual-functional peptide gatekeeper on mesoporous nanocontainers

2019 ◽  
Vol 43 (29) ◽  
pp. 11497-11502 ◽  
Author(s):  
Jeonghun Lee ◽  
Eun-Taex Oh ◽  
Hansol Kang ◽  
Jiwon Kim ◽  
Ha Gyeong Kim ◽  
...  
Keyword(s):  
Drug Release ◽  
Cyclic Peptide ◽  
Conformational Transformation ◽  
Stimuli Responsive ◽  
Specific Targeting ◽  
Dual Functional ◽  
Triggered Drug Release ◽  
Functional Peptide ◽  
Binding Sequence

For specific targeting of HER2 and triggered drug release by stimuli-responsive conformational transformation, we developed a dual-functional cyclic peptide gatekeeper containing a HER2-binding sequence on the surface of mesoporous nanocontainers.

Multi-stimuli responsive supramolecular hydrogels based on Fe3+ and diblock copolymer micelle complexation

2016 ◽  
Vol 7 (7) ◽  
pp. 1405-1412 ◽  
Author(s):  
Zhen Tao ◽  
Kang Peng ◽  
Yujiao Fan ◽  
Yunfei Liu ◽  
Haiyang Yang
Keyword(s):  
Carboxylic Acid ◽  
Uv Irradiation ◽  
Diblock Copolymer ◽  
Biomedical Application ◽  
Stimuli Responsive ◽  
Ferric Ions ◽  
Supramolecular Hydrogel ◽  
Carboxylic Acid Groups ◽  
Copolymer Micelle ◽  
Redox Agents

We report a multi-stimuli responsive supramolecular hydrogel with great potential for biomedical application, which was composed of the micelle-forming diblock copolymer and physically cross-linked by complexation between ferric ions and carboxylic acid groups, exhibiting gel–sol transition caused by UV irradiation, multidentate ligands (EDTA) and redox agents (Na2S2O4).

scholarly journals Rational Construction of a Responsive Azo-Functionalized Porous Organic Framework for CO2 Sorption

Molecules ◽  
2021 ◽  
Vol 26 (16) ◽  
pp. 4993
Author(s):  
Rongrong Yuan ◽  
Hao Sun ◽  
Hongming He
Keyword(s):  
Uv Irradiation ◽  
Co2 Adsorption ◽  
Adsorption Property ◽  
Sorption Isotherms ◽  
Bet Surface Area ◽  
Stimuli Responsive ◽  
Co2 Sorption ◽  
Rational Construction ◽  
Porous Organic Framework ◽  
Organic Framework

An azo-functionalized porous organic framework (denoted as JJU-1) was synthesized via FeCl3-promoted oxidative coupling polymerization. By virtue of a porous skeleton and a light/heat responsive azo functional group, this task-specific JJU-1 displays a reversible stimuli-responsive adsorption property triggered by UV irradiation and heat treatment. The initial Brunauer–Emmet–Teller (BET) surface area of this porous material is 467 m2 g–1. The CO2 sorption isotherms exhibit a slight decrease after UV irradiation because of the trans to cis conversion of the azo functional skeleton. It is worth mentioning that the responsive CO2 adsorption performance can be recycled for three cycles via alternating external stimuli, confirming the excellently reversible switchability of trans-to-cis isomerization and controllable CO2 adsorption.

scholarly journals Stapling of unprotected helical peptides via photo-induced intramolecular thiol–yne hydrothiolation

2016 ◽  
Vol 7 (5) ◽  
pp. 3325-3330 ◽  
Author(s):  
Yuan Tian ◽  
Jingxu Li ◽  
Hui Zhao ◽  
Xiangze Zeng ◽  
Dongyuan Wang ◽  
...  
Keyword(s):  
Uv Irradiation ◽  
Functional Group ◽  
Helical Conformation ◽  
Stapled Peptides ◽  
Helical Peptides ◽  
Rapid Access

A one component intramolecular thiol–yne macrocyclization is achieved upon UV irradiation to constrain short unprotected peptides into a helical conformation, providing rapid access to stapled peptides with satisfying functional group tolerance.

scholarly journals New Antibacterial Peptides from the Freshwater Mollusk Pomacea poeyana (Pilsbry, 1927)

Biomolecules ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1473
Author(s):  
Melaine González García ◽  
Armando Rodríguez ◽  
Annia Alba ◽  
Antonio A. Vázquez ◽  
Fidel E. Morales Vicente ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Galleria Mellonella ◽  
Random Coil ◽  
Helical Conformation ◽  
Moderate Activity ◽  
Human Pathogens ◽  
Spectra Analysis ◽  
Bacterial Membranes ◽  
Innate Defense

Antimicrobial peptides (AMPs) are biomolecules with antimicrobial activity against a broad group of pathogens. In the past few decades, AMPs have represented an important alternative for the treatment of infectious diseases. Their isolation from natural sources has been widely investigated. In this sense, mollusks are promising organisms for the identification of AMPs given that their immune system mainly relies on innate response. In this report, we characterized the peptide fraction of the Cuban freshwater snail Pomacea poeyana (Pilsbry, 1927) and identified 37 different peptides by nanoLC-ESI-MS-MS technology. From these peptide sequences, using bioinformatic prediction tools, we discovered two potential antimicrobial peptides named Pom-1 (KCAGSIAWAIGSGLFGGAKLIKIKKYIAELGGLQ) and Pom-2 (KEIERAGQRIRDAIISAAPAVETLAQAQKIIKGG). Database search revealed that Pom-1 is a fragment of Closticin 574 previously isolated from the bacteria Clostridium tyrobutyrium, and Pom-2 is a fragment of cecropin D-like peptide first isolated from Galleria mellonella hemolymph. These sequences were chemically synthesized and evaluated against different human pathogens. Interestingly, structural predictions of both peptides in the presence of micelles showed models that comprise two alpha helices joined by a short loop. The CD spectra analysis of Pom-1 and Pom-2 in water showed for both structures a high random coil content, a certain content of α-helix and a low β-sheet content. Like other described AMPs displaying a disordered structure in water, the peptides may adopt a helical conformation in presence of bacterial membranes. In antimicrobial assays, Pom-1 demonstrated high activity against the Gram-negative bacteria Pseudomonas aeruginosa and moderate activity against Klebsiella pneumoniae and Listeria monocytogenes. Neither of the two peptides showed antifungal action. Pom-1 moderately inhibits Zika Virus infection but slightly enhances HIV-1 infectivion in vitro. The evaluation of cell toxicity on primary human macrophages did not show toxicity on THP-1 cells, although slight overall toxicity was observed in high concentrations of Pom-1. We assume that both peptides may play a key role in innate defense of P. poeyana and represent promising antimicrobial candidates for humans.

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