Protein aggregation-inhibition: a therapeutic route from Parkinson's disease to sickle cell anemia

GF Martins, N Galamba - Critical Reviews in Biochemistry and …, 2023 - Taylor & Francis
Protein aggregation is implicated in multiple diseases, so-called proteinopathies, ranging
from neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease …

Evaluating sheep hemoglobins with MD simulations as an animal model for sickle cell disease

CE Kuczynski, CD Porada, A Atala, SS Cho… - Scientific Reports, 2024 - nature.com
Sickle cell disease (SCD) affects millions worldwide, yet there are few therapeutic options.
To develop effective treatments, preclinical models that recapitulate human physiology and …

The Use of Natural Products in the Treatment of Sickle Cell Disease

RG de Paula, HM Ribeiro, L de Melo Borges… - Revista Brasileira de …, 2024 - Springer
Sickle cell disease is the world's leading inherited genetic hemoglobinopathy, originating
from African peoples, characterized by the presence of more than 50% hemoglobin S in red …

Cyclic Peptides as Aggregation Inhibitors for Sickle Cell Disease

V Neto, BL Victor, N Galamba - Journal of Medicinal Chemistry, 2023 - ACS Publications
Sickle cell disease is a missense genetic disorder characterized by the aggregation of deoxy-
HbS into helical fibers that distort erythrocytes into a sickle-like shape. Herein, we …

Molecular dynamics of hemoglobin reveals structural alterations and explains the interactions driving sickle cell fibrillation

D Maity, D Pal - The Journal of Physical Chemistry B, 2021 - ACS Publications
In sickle cell anemia, deoxyhemoglobin deforms RBCs by forming fibrils inside that
disintegrate on oxygenation. We studied 100 ns long all-atom molecular dynamics (MD) for …

Multiscale MD simulations of wild‐type and sickle hemoglobin aggregation

MO Olagunju, J Loschwitz, OO Olubiyi… - Proteins: Structure …, 2022 - Wiley Online Library
Sickle cell disease is a hemoglobinopathy resulting from a point mutation from glutamate to
valine at position six of the β‐globin chains of hemoglobin. This mutation gives rise to …