Structural Stability Among Hybrid Antimicrobial Peptide Cecropin A(1–8)–Magainin 2(1–12) and Its Analogues: A Computational Approach

Senthilkumar, B.; Paul, D. Meshach; Srinivasan, E.; Rajasekaran, R.

doi:10.1007/s10876-017-1240-y

Cited by 5 publications

(8 citation statements)

References 60 publications

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“…developed the web‐based simulation platform MCPep that combines MC simulations with a coarse‐grained model of amino acids to enable fast simulations of peptide–membrane interactions . MCPep and the model it is based on have been used to explore the location and orientation of peptides in membranes, the free energy of association of peptides with membranes, and the helical content of peptides when interacting with membranes . Although modeling is helpful to explain experimental observations and predict expected interactions of peptides with membranes, it can be computationally intensive and still focuses on model lipid membrane; thus, modeling alone is not sufficient to fully discern peptide–membrane interactions.…”

Section: Introductionmentioning

confidence: 99%

Secondary structure of cell‐penetrating peptides during interaction with fungal cells

2018

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Cell-penetrating peptides (CPPs) are peptides that cross cell membranes, either alone or while carrying molecular cargo. Although their interactions with mammalian cells have been widely studied, much less is known about their interactions with fungal cells, particularly at the biophysical level. We analyzed the interactions of seven CPPs (penetratin, Pep-1, MPG, pVEC, TP-10, MAP, and cecropin B) with the fungal pathogen Candida albicans using experiments and molecular simulations. Circular dichroism (CD) of the peptides revealed a structural transition from a random coil or weak helix to an α-helix occurs for all peptides when the solvent is changed from aqueous to hydrophobic. However, CD performed in the presence of C. albicans cells showed that proximity to the cell membrane is not necessarily sufficient to induce this structural transition, as penetratin, Pep-1, and MPG did not display a structural shift in the presence of cells. Monte Carlo simulations were performed to further probe the molecular-level interaction with the cell membrane, and these simulations suggested that pVEC, TP-10, MAP, and cecropin B strongly penetrate into the hydrophobic domain of the membrane lipid bilayer, inducing a transition to an α-helical conformation. In contrast, penetratin, Pep-1 and MPG remained in the hydrophilic region without a shift in conformation. The experimental data and MC simulations combine to explain how peptide structure affects their interaction with cells and their mechanism of translocation into cells (direct translocation vs. endocytosis). Our work also highlights the utility of combining biophysical experiments, biological experiments, and molecular modeling to understand biological phenomena.

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Section: Introductionmentioning

confidence: 99%

Secondary structure of cell‐penetrating peptides during interaction with fungal cells

2018

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“…44,55,56 Peptide hybridization is an effective strategy for the design of novel functional peptides because hybrid peptides may combine the advantages of different native peptides. 62 In the current study, the hybrid peptide C-L was designed and manufactured by combining the active center of C 66,67 with the functional fragment of L 63,68 to improve the anti-inflammatory activity and reduce the cytotoxicity of the parental peptides. ProtParam analysis showed that the devised hybrid peptide had a higher net positive charge than the parental peptides, which suggested an improved anti-inflammatory potential.…”

Section: Discussionmentioning

confidence: 99%

“…After a detailed analysis of the primary physicochemical characteristics of the parental peptides, we designed and constructed a novel hybrid peptide C‐L by combining the active center of C and L, incorporating C (1‐8) 61,62,66,67 and L (17‐30) 63,64,68,69 …”

Section: Methodsmentioning

confidence: 99%

“…After a detailed analysis of the primary physicochemical characteristics of the parental peptides, we designed and constructed a novel hybrid peptide C-L by combining the active center of C and L, incorporating C (1-8) 61,62,66,67 and L (17-30). 63,64,68,69 Specifically, the charge and secondary structure of the predicted peptides were analyzed using ProtParam (ExPASy Proteomics Server: http://www.expasy.org/tools/ protp aram.…”

Section: Hybrid Peptide Designmentioning

confidence: 99%

“…It has been reported that C (1‐8) 61,62 and L (17‐30) 63,64 are the active centers of native AMPs. In the present study, we designed a hybrid peptide C (1‐8)‐L (17‐30) (hereafter, C‐L), by combining the active centers of the parental AMPs.…”

Section: Introductionmentioning

confidence: 99%

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A highly efficient hybrid peptide ameliorates intestinal inflammation and mucosal barrier damage by neutralizing lipopolysaccharides and antagonizing the lipopolysaccharide‐receptor interaction

Xin

Zhang

et al. 2020

FASEB j.

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Intestinal inflammatory disorders, such as inflammatory bowel disease, are major contributors to mortality and morbidity in humans and animals worldwide. While some native peptides have great potential as therapeutic agents against intestinal inflammation, potential cytotoxicity, anti-inciting action, and suppression of antiinflammatory activity may limit their development as anti-inflammatory agents. Peptide hybridization is an effective approach for the design and engineering of novel functional peptides because hybrid peptides combine the advantages and benefits of various native peptides. In the present study, a novel hybrid anti-inflammatory peptide that combines the active center of Cecropin A (C) and the core functional region of LL-37 (L) was designed [C-L peptide; C (1-8)-L (17-30)] through in silico analysis to reduce cytotoxicity and improve the anti-inflammatory activity of the parental peptides. The resulting C-L peptide exhibited lower cytotoxicity than either C or L peptides alone. C-L also exerted a protective effect against lipopolysaccharide (LPS)induced inflammatory responses in RAW264.7 macrophages and in the intestines of a mouse model. The hybrid peptide exhibited increased anti-inflammatory activity compared to the parental peptides. C-L plays a role in protecting intestinal tissue from damage, LPS-induced weight loss, and leukocyte infiltration. In addition, C-L reduces the expression levels of tumor necrosis factor-alpha (TNF-α), interleukin-6 2 | WEI Et al.

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Application of AMPs in the Food and Beverage Industry

Choudhary,

Shanu,

Devi

2024

Antimicrobial Peptides From Lactic Acid Bacteria

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Structural Stability Among Hybrid Antimicrobial Peptide Cecropin A(1–8)–Magainin 2(1–12) and Its Analogues: A Computational Approach

Cited by 5 publications

References 60 publications

Secondary structure of cell‐penetrating peptides during interaction with fungal cells

Secondary structure of cell‐penetrating peptides during interaction with fungal cells

A highly efficient hybrid peptide ameliorates intestinal inflammation and mucosal barrier damage by neutralizing lipopolysaccharides and antagonizing the lipopolysaccharide‐receptor interaction

Application of AMPs in the Food and Beverage Industry

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