Dresden 2020 – scientific programme

The DPG Spring Meeting in Dresden had to be cancelled! Read more ...

Parts | Days | Selection | Search | Updates | Downloads | Help

BP: Fachverband Biologische Physik

BP 19: Poster VII

BP 19.17: Poster

Tuesday, March 17, 2020, 14:00–16:00, P2/3OG

Domain Swapping in Crystallin Proteins Can Drive Early Stages of Cataract Formation — •Govardhan Reddy Patluri and Balaka Mondal — Indian Institute of Science, Bangalore, India

Crystallins (Crys) are densely packed, long-lived eye lens proteins responsible for the ocular functions of the lens. Physicochemical perturbations in the cellular environment disrupt the native state stability of Cry proteins and populate aggregation prone misfolded states. These misfolded states gradually accumulate to produce high molecular weight amorphous aggregates, which scatter visible light resulting in lens opacity or cataract. The molecular mechanism of cataract formation or structure of these aggregation prone precursors remain elusive to date. Using molecular dynamics simulations and coarse-grained protein model of human γC and γD Crys, we identified the aggregation prone misfolded states present in the unfolding pathways of these proteins. We further show that these partially misfolded conformations readily undergo dimerization by domain swapping revealing the early stages of aggregation leading to cataract formation.