Reducing Self-Assembly by Increasing Net Charge: Effect on Biological Activity of Mastoparan C

HB Thi Phuong, BL Huy, KN Van, ND Thi… - ACS Medicinal …, 2023 - ACS Publications
The ability of amphipathic peptides to arrange themselves in aqueous solutions, known as
self-assembly, has been found to reduce the effectiveness of these peptides in interacting …

Role of peptide self‐assembly in antimicrobial peptides

X Tian, F Sun, XR Zhou, SZ Luo… - Journal of Peptide …, 2015 - Wiley Online Library
Antimicrobial peptides (AMPs) are considered as potential antibiotic substitutes because of
their potent activities. Previous studies mainly focused on the effects of peptide charges and …

Improving the Antibacterial Activity of Tryptophan-Containing Peptide Nanostructures Through Self-Assembly

L Zhao, Z Liu, M Ji - International Journal of Peptide Research and …, 2023 - Springer
Antimicrobial peptides (AMPs) are frequently distributed in the tissues and organs of animals
to exhibit broad-spectrum activities against various pathogens, and thus to constitute the first …

Naturally occurring and artificially designed antimicrobial peptides: a comparative study of Mastoparan C and BP52

H Bui Thi Phuong, Y Do Hai, V Nguyen Huu… - Medicinal Chemistry …, 2024 - Springer
Antimicrobial peptides (AMPs) are naturally occurring molecules that play a vital role in the
innate immune responses of various organisms. Additionally, artificial AMPs are also …

Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X

JR Henriksen, T Etzerodt, T Gjetting, TL Andresen - PloS one, 2014 - journals.plos.org
The discovery of new anti-infective compounds is stagnating and multi-resistant bacteria
continue to emerge, threatening to end the “antibiotic era”. Antimicrobial peptides (AMPs) …

Computer-aided design of mastoparan-like peptides enables the generation of nontoxic variants with extended antibacterial properties

KGN Oshiro, ES Candido, LY Chan… - Journal of Medicinal …, 2019 - ACS Publications
Diverse peptides have been evaluated for their activity against pathogenic microorganisms.
Here, five mastoparan variants were designed based on mastoparan-L, among which two …

Self-assembled cationic amphiphiles as antimicrobial peptides mimics: role of hydrophobicity, linkage type, and assembly state

Y Zhang, A Algburi, N Wang, V Kholodovych… - … , Biology and Medicine, 2017 - Elsevier
Inspired by high promise using naturally occurring antimicrobial peptides (AMPs) to treat
infections caused by antimicrobial-resistant bacteria, cationic amphiphiles (CAms) were …

Deciphering the structure and mechanism of action of computer‐designed mastoparan peptides

KGN Oshiro, CDP Freitas, SB Rezende… - The FEBS …, 2024 - Wiley Online Library
Mastoparans are cationic peptides with multifunctional pharmacological properties.
Mastoparan‐R1 and mastoparan‐R4 were computationally designed based on native …

[PDF][PDF] Selective acylation enhances membrane charge sensitivity of the antimicrobial peptide mastoparan-x

T Etzerodt, JR Henriksen, P Rasmussen, MH Clausen… - Biophysical journal, 2011 - cell.com
The partitioning of the wasp venom peptide mastoparan-X (MPX) into neutral and negatively
charged lipid membranes has been compared with two new synthetic analogs of MPX …

Effects of salts on the self-assembly behavior and antibacterial activity of a surfactant-like peptide

C Chen, J Chen, Q Yu, J Zhang, X Niu, L Hao, L Yang… - Soft Matter, 2020 - pubs.rsc.org
Self-assembling peptides have become one of the most promising antibacterial agents due
to their superior properties, such as simple molecular composition, favorable assembly …