In molecular simulations, pramlintide exhibited a thermal helix-to-sheet conversion channel resembling human amylin.
In plain wordsComputer simulations showed a thermal helix-to-sheet conversion channel in pramlintide that resembled human amylin.
- Peptide
- Pramlintide (Symlin)
- Outcome
- Not applicableThermal helix-to-sheet conversion channel
- Study
n: not reported in source
Replica-exchange molecular dynamics of sIAPP- Outcome group
- Receptor activity and mechanism · Pharmacology
Source sentences
Our thermo-structural analyses show that sIAPP exhibits a thermal conversion channel of helices[Formula: see text]-sheets resembling hIAPP.
1 context sentence(design, population, supporting numbers)
we performed comparative assessments of rIAPP, sIAPP, and sIAPP+ using replica-exchange molecular dynamics (REMD) with an accurate combination of force field Charmm22* and explicit aqueous solvation TIP4P/Ew.
In this study, Pramlintide (Symlin) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Pramlintide (Symlin).