scholarly journals Effect of monovalent salt concentration and peptide secondary structure in peptide-micelle binding

RSC Advances ◽  
2021 ◽  
Vol 11 (58) ◽  
pp. 36836-36849
Author(s):  
Suvankar Ghosh ◽  
Gopal Pandit ◽  
Swapna Debnath ◽  
Sunanda Chatterjee ◽  
Priyadarshi Satpati
Keyword(s):  
Secondary Structure ◽  
Salt Concentration ◽  
Salt Sensitivity ◽  
Membrane Mimetic ◽  
Monovalent Salt ◽  
Peptide Secondary Structure

We report computational (∼14.2 μs of MD) and experimental (CD, fluorescence) investigations to examine the salt-sensitivity and the role of the peptide secondary structure on LL-14 binding to simple membrane mimetic systems.

scholarly journals Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges

Symmetry ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 812
Author(s):  
Markéta Pazderková ◽  
Václav Profant ◽  
Petr Maloň ◽  
Rina K. Dukor ◽  
Václav Čeřovský ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Tertiary Structure ◽  
Sodium Dodecyl ◽  
Disulfide Bridge ◽  
Biological Properties ◽  
Disulfide Bridges ◽  
Supporting Function ◽  
Bridge Pattern ◽  
Peptide Secondary Structure

We report an investigation of the role of disulfide bridges in the 27-residue antimicrobial peptide lasiocepsin (I) containing two disulfide groups (Cys8–Cys25, Cys17–Cys27) and three its analogs lacking one (II, III) or both (IV) native disulfides. Selective alternate incorporation of one or both disulfide bridges influences symmetry, conformation and biological properties of these peptides as demonstrated in their chiroptical (particularly Raman) properties. The effect of modifying the disulfide bridge pattern on the peptide secondary structure is investigated in water and in the presence of 2,2,2-trifluoroethanol and sodium dodecyl sulphate. A combination of experimental electronic and vibrational chiroptical data shows that both disulfide groups are necessary for stabilizing lasiocepsin secondary structure. While the Cys8–Cys25 disulfide group is important for sustaining lasiocepsin tertiary structure and maintaining its biological activity, the Cys17–Cys27 disulfide bridge has a supporting function consisting in reducing peptide flexibility.

Effect of High Salt Concentration on Ion Clustering and Transport in Polymer Solid Electrolytes: a Molecular Dynamics Study of PEO-LiTFSI

2018 ◽  
Author(s):  
Nicola Molinari ◽  
Jonathan P. Mailoa ◽  
Boris Kozinsky
Keyword(s):  
Polymer Electrolyte ◽  
Salt Concentration ◽  
Rational Design ◽  
Material System ◽  
Ion Dynamics ◽  
High Concentration ◽  
Anion Clusters ◽  
Poly Ethylene Oxide ◽  
Poly Ethylene

<div> <div> <div> <p>The model and analysis methods developed in this work are generally applicable to any polymer electrolyte/cation-anion combination, but we focus on the currently most prominent polymer electrolyte material system: poly(ethylene) oxide/Li- bis(trifluoromethane) sulfonamide (PEO + LiTFSI). The obtained results are surprising and challenge the conventional understanding of ionic transport in polymer electrolytes: the investigation of a technologically relevant salt concentration range (1 - 4 M) revealed the central role of the anion in coordinating and hindering Li ion movement. Our results provide insights into correlated ion dynamics, at the same time enabling rational design of better PEO-based electrolytes. In particular, we report the following novel observations. 1. Strong binding of the Li cation with the polymer competes with significant correlation of the cation with the salt anion. 2. The appearance of cation-anion clusters, especially at high concentration. 3. The asymmetry in the composition (and therefore charge) of such clusters; specifically, we find the tendency for clusters to have a higher number of anions than cations.</p> </div> </div> </div>

Effect of High Salt Concentration on Ion Clustering and Transport in Polymer Solid Electrolytes: a Molecular Dynamics Study of PEO-LiTFSI

2018 ◽  
Author(s):  
Nicola Molinari ◽  
Jonathan P. Mailoa ◽  
Boris Kozinsky
Keyword(s):  
Polymer Electrolyte ◽  
Salt Concentration ◽  
Rational Design ◽  
Material System ◽  
Ion Dynamics ◽  
High Concentration ◽  
Anion Clusters ◽  
Poly Ethylene Oxide ◽  
Poly Ethylene

<div> <div> <div> <p>The model and analysis methods developed in this work are generally applicable to any polymer electrolyte/cation-anion combination, but we focus on the currently most prominent polymer electrolyte material system: poly(ethylene) oxide/Li- bis(trifluoromethane) sulfonamide (PEO + LiTFSI). The obtained results are surprising and challenge the conventional understanding of ionic transport in polymer electrolytes: the investigation of a technologically relevant salt concentration range (1 - 4 M) revealed the central role of the anion in coordinating and hindering Li ion movement. Our results provide insights into correlated ion dynamics, at the same time enabling rational design of better PEO-based electrolytes. In particular, we report the following novel observations. 1. Strong binding of the Li cation with the polymer competes with significant correlation of the cation with the salt anion. 2. The appearance of cation-anion clusters, especially at high concentration. 3. The asymmetry in the composition (and therefore charge) of such clusters; specifically, we find the tendency for clusters to have a higher number of anions than cations.</p> </div> </div> </div>

RNA secondary structure dependence in METTL3–METTL14 mRNA methylation is modulated by the N-terminal domain of METTL3

2020 ◽  
Vol 402 (1) ◽  
pp. 89-98
Author(s):  
Nathalie Meiser ◽  
Nicole Mench ◽  
Martin Hengesbach
Keyword(s):  
Secondary Structure ◽  
Rna Binding ◽  
Specific Protein ◽  
Structure Dependence ◽  
Terminal Domain ◽  
Methylation Assay ◽  
A Site ◽  
Methylation Activity

AbstractN6-methyladenosine (m6A) is the most abundant modification in mRNA. The core of the human N6-methyltransferase complex (MTC) is formed by a heterodimer consisting of METTL3 and METTL14, which specifically catalyzes m6A formation within an RRACH sequence context. Using recombinant proteins in a site-specific methylation assay that allows determination of quantitative methylation yields, our results show that this complex methylates its target RNAs not only sequence but also secondary structure dependent. Furthermore, we demonstrate the role of specific protein domains on both RNA binding and substrate turnover, focusing on postulated RNA binding elements. Our results show that one zinc finger motif within the complex is sufficient to bind RNA, however, both zinc fingers are required for methylation activity. We show that the N-terminal domain of METTL3 alters the secondary structure dependence of methylation yields. Our results demonstrate that a cooperative effect of all RNA-binding elements in the METTL3–METTL14 complex is required for efficient catalysis, and that binding of further proteins affecting the NTD of METTL3 may regulate substrate specificity.

Pd(II) Complexes Mediated Hydrolytic Cleavage of Insulin B Chain: Regioselectivity and Influence of Peptide Secondary Structure

2000 ◽  
Vol 29 (9) ◽  
pp. 1030-1031 ◽  
Author(s):  
Xuemei Luo ◽  
Weijiang He ◽  
Yu Zhang ◽  
Zijian Guo ◽  
Longgen Zhu
Keyword(s):  
Secondary Structure ◽  
Hydrolytic Cleavage ◽  
Peptide Secondary Structure

Engineering bio-inspired peptide–polyurea hybrids with thermo-responsive shape memory behaviour

2021 ◽  
Author(s):  
Daseul Jang ◽  
Chase B. Thompson ◽  
Sourav Chatterjee ◽  
LaShanda T. J. Korley
Keyword(s):  
Hydrogen Bonding ◽  
Secondary Structure ◽  
Shape Memory ◽  
Shape Memory Behaviour ◽  
Peptide Secondary Structure

This paper highlights the influence of peptide secondary structure on the shape memory behaviour of peptidic polyureas, driven by hydrogen bonding arrangement and microphase-separated morphology.

Sign in / Sign up

Export Citation Format

Share Document