Antimicrobial peptide mechanism studied by scattering-guided molecular dynamics simulation
In an effort to combat rising antimicrobial resistance, our labs have rationally designed
cationic, helical, amphipathic antimicrobial peptides (AMPs) as alternatives to traditional …
cationic, helical, amphipathic antimicrobial peptides (AMPs) as alternatives to traditional …
Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ1–42 monomer differently than does the A2V mutation
The aggregation of amyloid-β (Aβ) peptides plays a crucial role in the etiology of Alzheimer's
disease (AD). Recently, it has been reported that an A2T mutation in Aβ can protect against …
disease (AD). Recently, it has been reported that an A2T mutation in Aβ can protect against …
Exploring the Barriers in the Aggregation of a Hexadecameric Human Prion Peptide through the Markov State Model
The prefibrillar aggregation kinetics of prion peptides are still an enigma. In this perspective,
we employ atomistic molecular dynamics (MD) simulations of the shortest human prion …
we employ atomistic molecular dynamics (MD) simulations of the shortest human prion …
Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulations
Knowledge of the detailed mechanism by which proteins such as human αB-crystallin and
human lysozyme inhibit amyloid beta (Aβ) peptide aggregation is crucial for designing …
human lysozyme inhibit amyloid beta (Aβ) peptide aggregation is crucial for designing …
Membrane-mediated neuroprotection by curcumin from amyloid-β-peptide-induced toxicity
A Thapa, BC Vernon, K De la Pena, G Soliz… - Langmuir, 2013 - ACS Publications
Amyloid-β peptide (Aβ)–membrane interactions have been implicated in the formation of
toxic oligomers that permeabilize membranes, allowing an influx of calcium ions and …
toxic oligomers that permeabilize membranes, allowing an influx of calcium ions and …
Molecular understanding of Aβ-hIAPP cross-seeding assemblies on lipid membranes
Amyloid-β (Aβ) and human islet polypeptide (hIAPP) are the causative agents responsible
for Alzheimer's disease (AD) and type II diabetes (T2D), respectively. While numerous …
for Alzheimer's disease (AD) and type II diabetes (T2D), respectively. While numerous …
Investigation of the interaction of amyloid β peptide (11–42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular …
Some amyloid related proteins/peptides are involved in aggregation and pore formation in
phospholipid membranes (cell membranes), which result in a variety of neurological …
phospholipid membranes (cell membranes), which result in a variety of neurological …
[HTML][HTML] Atomistic-level study of the interactions between hIAPP protofibrils and membranes: Influence of pH and lipid composition
The pathology of type 2 diabetes mellitus is associated with the aggregation of human islet
amyloid polypeptide (hIAPP) and aggregation-mediated membrane disruption. The …
amyloid polypeptide (hIAPP) and aggregation-mediated membrane disruption. The …
Characterisation of the structure and oligomerisation of islet amyloid polypeptides (IAPP): a review of molecular dynamics simulation studies
Human islet amyloid polypeptide (hIAPP) is a naturally occurring, intrinsically disordered
protein whose abnormal aggregation into amyloid fibrils is a pathological feature in type 2 …
protein whose abnormal aggregation into amyloid fibrils is a pathological feature in type 2 …
Alzheimer's disease: which type of amyloid-preventing drug agents to employ?
H Jang, L Connelly, FT Arce… - Physical Chemistry …, 2013 - pubs.rsc.org
The current paradigm in the amyloid hypothesis brands small β-amyloid (Aβ) oligomers as
the toxic species in Alzheimer's disease (AD). These oligomers are fibril-like; contain β-sheet …
the toxic species in Alzheimer's disease (AD). These oligomers are fibril-like; contain β-sheet …