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PubMed Publications| Keyword search (4,163 papers available) |  |
"Mansbach RA" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Revealing pH-dependent antimicrobial peptide, GL13K, characteristics: A constant pH molecular dynamics study | Hamidabad MN; Mansbach RA; | 41256587 PHYSICS |
| 2 | In Silico Study of the Early Stages of Aggregation of β-Sheet Forming Antimicrobial Peptide GL13K | Hamidabad MN; Watson NA; Wright LN; Mansbach RA; | 38572930 PHYSICS |
| 3 | Identification of Residues Potentially Involved in Optical Shifts in the Water-Soluble Chlorophyll a-Binding Protein through Molecular Dynamics Simulations | Mai M; Zazubovich V; Mansbach RA; | 38299975 PHYSICS |
| 4 | Exploring the Role of Glycans in the Interaction of SARS-CoV-2 RBD and Human Receptor ACE2 | Nguyen K; Chakraborty S; Mansbach RA; Korber B; Gnanakaran S; | 34067878 PHYSICS |
| 5 | Effects of pH on an IDP conformational ensemble explored by molecular dynamics simulation. | Lindsay RJ, Mansbach RA, Gnanakaran S, Shen T | 33581430 PHYSICS |
| Title: | In Silico Study of the Early Stages of Aggregation of β-Sheet Forming Antimicrobial Peptide GL13K | ||||
| Authors: | Hamidabad MN, Watson NA, Wright LN, Mansbach RA | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/38572930/ | ||||
| DOI: | 10.1002/cbic.202400088 | ||||
| Publication: | Chembiochem : a European journal of chemical biology | ||||
| Keywords: | antimicrobial peptides; biophysics; molecular dynamics simulation; | ||||
| PMID: | 38572930 | Category: | Date Added: | 2024-04-04 | |
| Dept Affiliation: |
PHYSICS
1 Physics Department, Concordia University, Montréal, QC, H4B 1R6, Canada. |
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Description: |
Antimicrobial peptides (AMPs) are of growing interest as potential candidates that may offer more resilience against antimicrobial resistance than traditional antibiotic agents. In this article, we perform the first in silico study of the synthetic ß sheet-forming AMP GL13K. Through atomistic simulations of single and multi-peptide systems under different conditions, we are able to shine a light on the short timescales of early aggregation. We find that isolated peptide conformations are primarily dictated by sequence rather than charge, whereas changing charge has a significant impact on the conformational free energy landscape of multi-peptide systems. We demonstrate that the loss of charge-charge repulsion is a sufficient minimal model for experimentally observed aggregation. Overall, our work explores the molecular biophysical underpinnings of the first stages of aggregation of a unique AMP, laying necessary groundwork for its further development as an antibiotic candidate. |
