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Trollmann, M. F.

Publications and source records attributed to Trollmann, M. F..

2 recordsLinked to original sources

Large phospholipid-number asymmetry is not required to reproduce plasma membrane physical properties

Plasma membranes are compositionally asymmetric, but whether this lipid-type asymmetry is accompanied by a substantial phospholipid-number imbalance between leaflets remains debated. Here, we use microsecond all-atom molecular dynamics simulations to compare human red blood cell plasma membrane models with either strong phospholipid-number asymmetry and exoplasmic cholesterol enrichment or near-symmetric phospholipid and cholesterol numbers but preserved lipid-type asymmetry. Both asymmetric models reproduce a densely packed, ordered exoplasmic leaflet and a more fluid cytoplasmic leaflet. Strong phospholipid-number asymmetry, however, drives extensive cholesterol enrichment in the exoplasmic leaflet and amplifies membrane asymmetry, leading to large cholesterol-rich clusters, enhanced shallow hydrophobic exposure, reduced exoplasmic lipid mobility, lower ethanol permeability, and increased area compressibility. Comparison with available diffusion and alcohol-permeability measurements indicates that the strongly asymmetric model overestimates the immobilization and barrier properties of the exoplasmic leaflet, whereas the near-symmetric-number model better captures these dynamic observables. Our results suggest that lipid-type asymmetry is sufficient to reproduce many physical hallmarks of plasma membranes without requiring a large phospholipid-number imbalance.

biophysics↗

Mechanistic Insight into pH-Driven Phase Transition of Lipid Nanoparticles

The functionality of lipid nanoparticles (LNPs) as delivery systems in mRNA-based therapeutics is intricately linked to the protonation behavior of their aminolipid components. This study employs large-scale constant-pH molecular dynamics (CpHMD) simulations to decode the environment-dependent pKa of aminolipids in the Comirnaty lipid formulation, providing a detailed view of their pH-dependent structural dynamics. Our results reveal a significant shift in the apparent pKa of the aminolipid ALC-0315, from an intrinsic value of 9.3 in water to 4.9 within the LNP environment. This shift arises from the interplay between lipid reorganization and local electrostatic interactions, resulting in distinct protonation states across the LNP core and surface. At low pH, protonated aminolipids dominate the LNP surface, promoting efficient mRNA encapsulation, whereas at neutral pH, deprotonated aminolipids migrate to the hydrophobic core, driving structural stabilization. Notably, the localized pKa of aminolipids varies significantly with their position, decreasing from near-surface regions (7 to 8) to the hydrophobic core ([≤]4). These findings elucidate the molecular mechanisms underpinning LNP phase transitions and highlight the key role of pKa shifts for the design of aminolipids and for optimizing LNP compositions for enhanced therapeutic delivery. This study bridges experimental observations with molecular-level insights, advancing the rational development of next-generation lipid-based nanocarriers.

biophysics↗