Aug 2026· Journal of Membrane Biology· Vol 259· 0 citations· 40 references
Medicine
TL;DR
It is demonstrated that both peptides can be inserted into the preformed vesicles, and that the free energy difference between their partitioning is < 1 kcal/mol, disproving the hypothesis that KALP peptides are kinetically trapped and opening the doors for using this system for thermodynamic measurements to further test the additivity assumptions implicit in applications of hydrophobicity scales.
A lipid-shell modification to the protocol for assigning a residue’s character on a hydropathy (PARCH) scale is presented, in which the protein’s first hydration shell is enclosed by a lipid boundary layer during thermal annealing to establish a computationally affordable and physically meaningful approach to quantifyi...
Ratnakshi Mandal, S. Nangia· Journal of Physical Chemistr...· 0 citations
The results reveal an unexpected dependence of partitioning energetics on both bilayer elastic energy and lipid packing defects, demonstrating how subtle changes in membrane physical properties could redirect protein folding pathways and thermodynamics.
Swadha Gupta, R. Mahalakshmi· Biochemistry· 0 citations
The model provides a computationally efficient framework for studying conformational ensembles and assembly of proteins at bilayer–water interfaces and is validated against Wimley–White free energies of transfer of hydrophobic peptides and against an experimentally refined conformational ensemble of a flexible membrane...
Together, these results link peptide sequence to pore-rim localization, lipid reorganization, and ultimately line-tension reduction, providing molecular design principles for α-helical peptides that stabilize permeable membrane states.
Together, these results demonstrate that the amphipathic helix of FtsL functions as a membrane-interacting element that stabilizes the protein in the membrane environment and mediates the recruitment of downstream proteins to the divisome for Mtb cell division.
Jiaxing Fan, Ramesh Prasad, Rongfu Zhang et al.· Journal of the American Chem...· 0 citations
This study illustrates how subtle residue-localized conformational bias can affect the overall protein conformational dynamics influencing protein-protein interactions that are important for cellular functions and related to diseases.
Abir Ben Bouzayene, M. Sai, Alexis Jouin et al.· Angewandte Chemie· 0 citations
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