Evaluating the effects of hydrophobic and cationic residues on antimicrobial peptide self-assembly

Soft Matter ◽  
2021 ◽  
Vol 17 (16) ◽  
pp. 4445-4451
Author(s):  
Fengyi Cao ◽  
Gangqing Ma ◽  
Meng Song ◽  
Genxing Zhu ◽  
Lin Mei ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Self Assembly ◽  
Peptide Derivatives ◽  
Cationic Residues ◽  
Secondary Conformation

Four PAF26 peptide derivatives were used to study the effects of hydrophobic and cationic residues on self-assembly behaviours. It was found that peptide with different number of hydrophobic and cationic residues had different secondary conformation and microstructure.

scholarly journals Self-assembly and hydrogel formation ability of Fmoc-dipeptides comprising α-methyl-L-phenylalanine

2020 ◽  
Vol 52 (8) ◽  
pp. 923-930 ◽  
Author(s):  
Hanae Arakawa ◽  
Kumi Takeda ◽  
Sayuri L. Higashi ◽  
Aya Shibata ◽  
Yoshiaki Kitamura ◽  
...  
Keyword(s):  
Self Assembly ◽  
Network Formation ◽  
Aqueous Media ◽  
Three Dimensional ◽  
The Self ◽  
Methyl Groups ◽  
Marked Influence ◽  
Hydrogel Network ◽  
Hydrogel Formation ◽  
Peptide Derivatives

AbstractVarious biofunctional hydrogel materials can be fabricated in aqueous media through the self-assembly of peptide derivatives, forming supramolecular nanostructures and their three-dimensional networks. In this study, we describe the self-assembly of new Fmoc-dipeptides comprising α-methyl-L-phenylalanine. We found that the position and number of methyl groups introduced onto the α carbons of the Fmoc-dipeptides by α-methyl-L-phenylalanine have a marked influence on the morphology of the supramolecular nanostructure as well as the hydrogel (network) formation ability.

Antimicrobial activity and self-assembly behavior of antimicrobial peptide chensinin-1b with lipophilic alkyl tails

2018 ◽  
Vol 150 ◽  
pp. 546-558 ◽  
Author(s):  
Weibing Dong ◽  
Ziang Liu ◽  
Liying Sun ◽  
Cui Wang ◽  
Yue Guan ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptide ◽  
Self Assembly ◽  
Assembly Behavior

scholarly journals Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
V. Castelletto ◽  
P. Ryumin ◽  
R. Cramer ◽  
I. W. Hamley ◽  
M. Taylor ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Self Assembly ◽  
Amyloid Beta Peptide ◽  
Cytotoxicity Activity ◽  
Beta Peptide ◽  
Peptide Derivatives

Enzyme-instructed self-assembly of peptide derivatives to form nanofibers and hydrogels

Biopolymers ◽  
2010 ◽  
Vol 94 (1) ◽  
pp. 19-31 ◽  
Author(s):  
Yuan Gao ◽  
Zhimou Yang ◽  
Yi Kuang ◽  
Man-Lung Ma ◽  
Jiayang Li ◽  
...  
Keyword(s):  
Self Assembly ◽  
Peptide Derivatives

In situ hydrogelation of bicalutamide-peptide conjugates at prostate tissue for smart drug release based on pH and enzymatic activity

Nanoscale ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 5030-5037 ◽  
Author(s):  
Suyun He ◽  
Leixia Mei ◽  
Can Wu ◽  
Mingtao Tao ◽  
Ziran Zhai ◽  
...  
Keyword(s):  
Drug Release ◽  
Enzymatic Activity ◽  
Self Assembly ◽  
Prostate Tissue ◽  
Cancer Drug ◽  
Peptide Conjugates ◽  
Anti Cancer ◽  
Peptide Derivatives ◽  
Smart Drug

The integration of an anti-cancer drug bicalutamide with tissue-specific supramolecular self-assembly of peptide derivatives yielded in situ hydrogelation at prostate tissue for smart drug release.

scholarly journals Self-assembly of glycerol monooleate with the antimicrobial peptide LL-37: a molecular dynamics study

RSC Advances ◽  
2020 ◽  
Vol 10 (14) ◽  
pp. 8291-8302 ◽  
Author(s):  
R. Innocenti Malini ◽  
M. Zabara ◽  
M. Gontsarik ◽  
K. Maniura-Weber ◽  
R. M. Rossi ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Antimicrobial Peptide ◽  
Molecular Dynamics Simulations ◽  
Self Assembly ◽  
Hydrophobic Interactions ◽  
Dynamics Simulations ◽  
Glycerol Monooleate

Molecular dynamics simulations of glycerol-monooleate (GMO)/LL-37 nanocarriers show that hydrophobic interactions among the molecules drive the formation of GMO/LL-37 micelles.

scholarly journals Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity

2019 ◽  
Vol 1 (12) ◽  
pp. 4679-4682 ◽  
Author(s):  
Zhou Ye ◽  
Conrado Aparicio
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Antimicrobial Peptide ◽  
Amino Acid Substitution ◽  
Self Assembly ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid ◽  
Hydrophobic Amino Acids ◽  
Assembly Performance

Single amino acid substitution of charged or hydrophobic amino acids of a designer antimicrobial peptide modulated structural and self-assembly performance and potency.

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