Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors

García-Morales, Abigail; Balleza, Daniel

doi:10.1007/s00239-023-10140-1

J Mol Evol

2023

DOI: 10.1007/s00239-023-10140-1

|View full text |Cite

Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors

Abigail García-Morales,

Daniel Balleza

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2024

Publication Types

Select...

Article1

Relationship

Self Cite0

Independent1

Authors

Journals

Cited by 1 publication

References 102 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Conformational Flexibility and Net Charge are Key Determinants for the Antimicrobial Activity of Peptide Uy234 Against Multidrug-resistant Bacteria

Salazar-Hernández,

Juárez-González,

Bustamante

et al. 2024

Int J Pept Res Ther

View full text Add to dashboard Cite

Background The antimicrobial activity of two peptides, Uy234 derived from the venom of the scorpion Urodacus yaschenkoi and a consensus peptide QnCs-Buap, was evaluated. We tested different pathogenic bacteria: Acinetobacter baumannii, Klebsiella pneumoniae, Salmonella enterica, Bacillus subtilis, Enterococcus spp. and Staphylococcus aureus, including one methicillin resistant (MRSA) and two multidrug resistant (MDR) clinical isolates. In contrast to the QnCs-Buap peptide, Uy234 showed relevant growth inhibitory activity on A. baumannii and B. subtilis, and mostly on S. aureus strains. Objective The present research focused on elucidating the mechanism for this antibacterial activity. Methodology We carried out an in-depth analysis of the composition, structure, flexibility, and physicochemical properties of both peptides. Results We found a crucial role of the C-terminal amide and composition in favoring the formation of a dense H-bond network in the Uy234 peptide. This H-bonding network slightly stiffens the peptide and keeps it in a preordered conformation in the aqueous phase. Conclusions We hypothesize that, given that Uy234 is a very short peptide (18 aa), it could have a destabilizing effect and favor micellization phenomena instead forming pores. In contrast, the QnCs-Buap peptide (13 aa), having only the positive charge at the N-terminal end and being significantly more hydrophobic and rigid, is not capable of overcoming the energy barrier to disturb the membrane. We propose that Uy234 peptide can be a scaffold to develop new derivatives with high potential against infections caused by diverse multidrug-resistant bacteria. Graphical Abstract

show abstract

Conformational Flexibility and Net Charge are Key Determinants for the Antimicrobial Activity of Peptide Uy234 Against Multidrug-resistant Bacteria

Salazar-Hernández,

Juárez-González,

Bustamante

et al. 2024

Int J Pept Res Ther

View full text Add to dashboard Cite

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Exploring Flexibility and Folding Patterns Throughout Time in Voltage Sensors

Cited by 1 publication

References 102 publications

Conformational Flexibility and Net Charge are Key Determinants for the Antimicrobial Activity of Peptide Uy234 Against Multidrug-resistant Bacteria

Conformational Flexibility and Net Charge are Key Determinants for the Antimicrobial Activity of Peptide Uy234 Against Multidrug-resistant Bacteria

Contact Info

Product

Resources

About