Impact of chemical modifications on the antimicrobial and hemolytic activity of helical amphipathic peptide Lasioglossin LL-III

Bui Thi Phuong, Hai; Le Uyen, Chi; Doan Ngan, Hoa; Luong Xuan, Huy

doi:10.1007/s00726-023-03326-w

Amino Acids

2023

DOI: 10.1007/s00726-023-03326-w

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Impact of chemical modifications on the antimicrobial and hemolytic activity of helical amphipathic peptide Lasioglossin LL-III

Hai Bui Thi Phuong,

Chi Le Uyen,

Hoa Doan Ngan

et al.

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Cited by 3 publications

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“…While numerous chemical strategies have been employed to enhance the pharmaceutical properties of antimicrobial peptides (AMPs), limited efforts have specifically targeted the modulation of peptide self-assembly. Recent studies have suggested that increased hydrophobicity via lipidation of AMPs may result in higher self-assembly, whereas enhanced cationic charge could decrease this tendency .…”

mentioning

confidence: 99%

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

Thi Phuong,

Huy,

Van

et al. 2023

ACS Med. Chem. Lett.

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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 with cell membranes. Therefore, minimizing their tendency to self-assemble could be a potential strategy for enhancing the pharmacological properties of antimicrobial peptides (AMPs). To explore this idea, this study prepared a series of natural peptides mastoparan C (MPC) with increased net charge and hydrophilicity via alanine-to-lysine substitution and investigated the impact on the biological activity. The preliminary data suggested the influence of both the overall positive charge and the position of a lysine residue on the selfassembly of MPC and its derivatives. Besides, the analogue MPC-A5K,A8K displayed higher anticancer activity and comparable antimicrobial activity with significantly lower hemolysis than MPC. Hence, reducing self-assembly by expanding the cationic area could be a promising approach for developing potent and selective AMPs.

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mentioning

confidence: 99%

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

Thi Phuong,

Huy,

Van

et al. 2023

ACS Med. Chem. Lett.

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The amphipathic design in helical antimicrobial peptides

Bui Thi Phuong,

Doan Ngan,

Le Huy

et al. 2024

ChemMedChem

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Amphipathicity is a critical characteristic of helical antimicrobial peptides (AMPs). The hydrophilic region, primarily composed of cationic residues, plays a pivotal role in the initial binding to negatively charged components on bacterial membranes through electrostatic interactions. Subsequently, the hydrophobic region interacts with hydrophobic components, inducing membrane perturbation, ultimately leading to cell death, or inhibiting intracellular function. Due to the extensive diversity of natural and synthetic AMPs with regard to the design of amphipathicity, it is complicated to study the structure‐activity relationships. Therefore, this work aims to categorize the common amphipathic design and investigate their impact on the biological properties of AMPs. Besides, the connection between current structural modification approaches and amphipathic styles was also discussed.

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

Bui Thi Phuong,

Do Hai,

Nguyen Huu

et al. 2024

Med Chem Res

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Impact of chemical modifications on the antimicrobial and hemolytic activity of helical amphipathic peptide Lasioglossin LL-III

Cited by 3 publications

References 54 publications

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

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

The amphipathic design in helical antimicrobial peptides

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

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