A coarse graining approach to Gliadin p31-43 peptide aggregation. (Presentación oral)

BARRERA GUISASOLA, EXEQUIEL E.; PANTANO, SERGIO

Pelotas

Workshop; X Workshop in Complexity of Water and Other Liquids.; 2019

Poly glutamine and glutamine-rich peptides play a central role in aplethora of pathological aggregation events. However, biophysicalcharacterization of soluble oligomers ―the most toxic speciesinvolved in these processes― remains elusive due to theirstructural heterogeneity and dynamical nature. Here, we exploit thehigh spatio-temporal resolution of simulations as a computationalmicroscope to characterize the aggregation propensity and morphologyof a series of polyglutamine and glutamine-rich peptides. Comparativeanalysis of ab-initio aggregation pinpointed a double role forglutamines. In the first phase, glutamines mediate seeding by pairingmonomeric peptides, which serve as primers for higher-ordernucleation. According to the glutamine content, these lowmolecular-weight oligomers may then proceed to create largeraggregates. Once within the aggregates, buried glutamines continue toplay a role in their maturation by optimizing solvent-protectedhydrogen bonds networks.p { margin-bottom: 0.1in; direction: ltr; color: #00000a; line-height: 120%; text-align: left; orphans: 2; widows: 2 }p.western { font-family: "Liberation Serif", serif; font-size: 12pt; so-language: en-US }p.cjk { font-family: "WenQuanYi Zen Hei Sharp"; font-size: 12pt; so-language: zh-CN }p.ctl { font-family: "Lohit Devanagari"; font-size: 12pt; so-language: hi-IN }a:link { so-language: uz-Cyrl-UZ }