Toward Light-Controlled Supramolecular Peptide Dimerization

2021 ◽  
Author(s):  
Rita J. Fernandes ◽  
Patricia Remón ◽  
Artur J. Moro ◽  
André Seco ◽  
Ana S. D. Ferreira ◽  
...  
Keyword(s):  
Peptide Dimerization

Dimerization of the Antimicrobial Peptide Polyphemusin I into One Polypeptide Chain: Theoretical and Practical Consequences

2019 ◽  
Vol 35 (5) ◽  
pp. 36-41
Author(s):  
V.A. Zenin ◽  
E.G. Sadykhov ◽  
A.N. Fedorov
Keyword(s):  
Antimicrobial Peptides ◽  
Pore Formation ◽  
Lipid Membrane ◽  
Polypeptide Chain ◽  
Unique Identifier ◽  
Bacterial Cultures ◽  
In Series ◽  
The Russian Federation ◽  
Peptide Dimerization ◽  
Putative Mechanism

A strategy of sequential dimerization of monomers of antimicrobial peptides (AMPs) into one polypeptide chain has been implemented on the example of a beta-structural AMP polyphemusin I which is one of the most effective candidate for use as an antibiotic. The possible polyphemusin I monomer and dimer structures in lipid membrane were studied in this work via molecular modeling. To this end, these molecules were chemically synthesized so that the dimer represented two monomers connected in series into one polypeptide chain with a flexible linker. The antimicrobial effects of monomer and dimer were then tested on various bacterial cultures, and their similarity was shown. Therefore, we can conclude that the pore formation is not a putative mechanism of the polyphemusin I action. antimicrobial peptides, peptide dimerization, mechanism of antimicrobial action, polyphemusin The work was supported by the Ministry of Science and Higher Education of the Russian Federation (Project Unique Identifier RFMEFI57517X0151).

scholarly journals Quantitative Heterodimerization of Aromatic Peptides through Host-Enhanced Polar–π Interactions for On-Resin Recognition

2021 ◽  
Author(s):  
Xiaoyi Chen ◽  
Zehuan Huang ◽  
Guanglu Wu ◽  
Kamil Sokłolowski ◽  
Katherine King ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Supramolecular Systems ◽  
Π Interactions ◽  
High Binding ◽  
Peptide Mixture ◽  
Peptide Dimerization ◽  
High Binding Affinity

Peptide dimerization plays an important role in both natural and artificial supramolecular systems. A major challenge to date is the quantitative heterodimerization of two peptides without formation of homodimers. Here, we employ a macrocyclic host to simultaneously encapsulate a canonical aromatic peptide and a non-canonical perfluorophenylalanine-containing peptide through polar–π interactions, thus forming an unprecedented new series of heteropeptide dimers with high binding affinity. This new peptide heterodimerization was applied to on-resin recognition and separation of aromatic peptides in a peptide mixture exhibiting over 95% isolation purity. This research unveils a generic approach to exploit quantitative heteropeptide dimers for the design of supramolecular (bio)systems.

Synthetic de novo designed polypeptides for control of nanoparticle assembly and biosensing

2007 ◽  
Vol 35 (3) ◽  
pp. 532-534 ◽  
Author(s):  
D. Aili ◽  
K. Enander ◽  
L. Baltzer ◽  
B. Liedberg
Keyword(s):  
Gold Nanoparticles ◽  
De Novo ◽  
Particle Aggregation ◽  
Helix Bundle ◽  
Helix Loop Helix ◽  
Synthetic Polypeptides ◽  
Convenient Route ◽  
Four Helix Bundle ◽  
Peptide Dimerization ◽  
Planar Substrates

This contribution describes how de novo designed synthetic helix–loop–helix polypeptides are utilized to control the assembly of gold nanoparticles and as scaffolds for biosensing. The synthetic polypeptides are designed to fold into a four-helix bundle upon dimerization. When immobilized on gold nanoparticles, dimerization and folding occur between peptides on neighbouring particles as an effect of particle aggregation and the folded polypeptides are rigid enough to keep the particles separated at a distance corresponding to the size of the four-helix bundle. Moreover, peptide dimerization offers a convenient route to assemble nanoparticles into hybrid multilayers on planar substrates. The drastic change in the resonance conditions of the localized nanoparticle surface plasmon upon particle aggregation is shown to be useful for optical detection of biomolecular interactions.

scholarly journals Dimerization of Antimicrobial Peptides: A Promising Strategy to Enhance Antimicrobial Peptide Activity

2019 ◽  
Vol 26 (2) ◽  
pp. 98-107 ◽  
Author(s):  
Esteban N. Lorenzon ◽  
Julia P. Piccoli ◽  
Norival A. Santos-Filho ◽  
Eduardo M. Cilli
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Mechanism Of Action ◽  
Antimicrobial Agents ◽  
Membrane Disruption ◽  
Promising Strategy ◽  
Peptide Dimerization ◽  
The Relationship ◽  
Intracellular Targets ◽  
Global Health Problem

Antimicrobial resistance is a global health problem with strong social and economic impacts. The development of new antimicrobial agents is considered an urgent challenge. In this regard, Antimicrobial Peptides (AMPs) appear to be novel candidates to overcome this problem. The mechanism of action of AMPs involves intracellular targets and membrane disruption. Although the exact mechanism of action of AMPs remains controversial, most AMPs act through membrane disruption of the target cell. Several strategies have been used to improve AMP activity, such as peptide dimerization. In this review, we focus on AMP dimerization, showing many examples of dimerized peptides and their effects on biological activity. Although more studies are necessary to elucidate the relationship between peptide properties and the dimerization effect on antimicrobial activity, dimerization constitutes a promising strategy to improve the effectiveness of AMPs.

Effects of peptide dimerization on pore formation: Antiparallel disulfide-dimerized magainin 2 analogue

Biopolymers ◽  
2001 ◽  
Vol 58 (4) ◽  
pp. 437-446 ◽  
Author(s):  
Toshiaki Hara ◽  
Hiroaki Kodama ◽  
Michio Kondo ◽  
Kaori Wakamatsu ◽  
Akemi Takeda ◽  
...  
Keyword(s):  
Pore Formation ◽  
Peptide Dimerization
Sign in / Sign up

Export Citation Format

Share Document