BEGIN:VCALENDAR VERSION:2.0 PRODID:www.dresden-science-calendar.de METHOD:PUBLISH CALSCALE:GREGORIAN X-MICROSOFT-CALSCALE:GREGORIAN X-WR-TIMEZONE:Europe/Berlin BEGIN:VTIMEZONE TZID:Europe/Berlin X-LIC-LOCATION:Europe/Berlin BEGIN:DAYLIGHT TZNAME:CEST TZOFFSETFROM:+0100 TZOFFSETTO:+0200 DTSTART:19810329T030000 RRULE:FREQ=YEARLY;INTERVAL=1;BYMONTH=3;BYDAY=-1SU END:DAYLIGHT BEGIN:STANDARD TZNAME:CET TZOFFSETFROM:+0200 TZOFFSETTO:+0100 DTSTART:19961027T030000 RRULE:FREQ=YEARLY;INTERVAL=1;BYMONTH=10;BYDAY=-1SU END:STANDARD END:VTIMEZONE BEGIN:VEVENT UID:DSC-22781 DTSTART;TZID=Europe/Berlin:20260701T110000 SEQUENCE:1781328944 TRANSP:OPAQUE DTEND;TZID=Europe/Berlin:20260701T120000 URL:https://dresden-science-calendar.de/calendar/de/detail/22781 LOCATION:TUD CRTD\, Fetscherstraße 10501307 Dresden SUMMARY:Lee: Interplay between Phase Separation and Amyloid Formation of TD P-43 C-terminal domain CLASS:PUBLIC DESCRIPTION:Speaker: Jennifer Lee\nInstitute of Speaker: National Heart\, B lood\, and Lung Institute\, USA\nTopics:\n\n Location:\n Name: TUD CRTD ( )\n Street: Fetscherstraße 105\n City: 01307 Dresden\n Phone: +49 (0)3 51 458 82052\n Fax: +49 (0)351 458 82059 \nDescription:

We are pleased to announce a new PoL Seminar by Jennifer Lee from the N ational Heart\, Blood\, and Lung Institute\, USA

When? &\;nbsp\;Wednesday\, 1. July 2026\, 11:00 am
Where? CRTD auditorium left

Abstract:

Liquid-li quid phase-separation (LLPS) is a physical phenomenon in which biomolecule s spontaneously form metastable\, concentrated droplet phases. Understandi ng the link between LLPS and the disease-related process of amyloid format ion has attracted significant interest. Here\, we investigated the relatio nship between LLPS and aggregation of the C-terminal domain (CTD) of the t ransactive response DNA binding protein of 43 kD (TDP-43). TDP-43CTD is fo und in cytoplasmic inclusions associated with amyotrophic lateral sclerosi s and frontotemporal lobar dementia. A prevailing hypothesis suggests that a liquid-to-solid transition occurs during TDP-43CTD droplet maturation\, involving formation of β-sheet–rich\, amyloid-like pathological aggreg ates. To evaluate how protein secondary structure evolves temporally and s patially within individual condensates\, we employed label-free Raman spec tral imaging to assess kinetics and spatial heterogeneity of β-sheet deve lopment at the individual droplet level. To obtain site-specific informati on\, we substituted a Raman-active\, environmentally-sensitive unnatural a mino acid\, 4-ethynylphenylalanine\, at various aromatic sites via amber c odon suppression. Despite the development of β-sheet structure\, conforme rs within aged droplets are distinguishable from fibrillar aggregates as s hifts in the alkyne band indicate local environmental differences between the two forms. Interestingly\, both aged droplets and fibrillar aggregates exhibited distinctive spectral features in distal N- and C-terminal sites outside the structured amyloid core. Importantly\, our results reveal fib ril polymorphism in the C-terminal region. The coexistence of solidified d roplets and amyloid fibrils indicates that these structures represent dist inct pathways. While droplets are amyloid-like\, amyloid fibrils can form independently of droplets\, challenging the paradigm that phase separation is an obligate step in amyloid formation.

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Everybody is very welcome. Don’t miss a great opportunity to join the seminar!

Please note: This seminar is going to take place in person at CRTD and will not be streamed via Zoom.

DTSTAMP:20260613T174033Z CREATED:20260319T063631Z LAST-MODIFIED:20260613T053544Z END:VEVENT END:VCALENDAR