# The molecular determinants of surface-templated self-association of intrinsically disordered proteins

> **NIH NIH R35** · UNIVERSITY OF SOUTHERN CALIFORNIA · 2023 · $413,864

## Abstract

Project Summary
The long-term goal of our research program is to utilize new techniques and paradigms to understand the
molecular determinants of physiological and disease-relevant phenomena associated with intrinsically
disordered proteins (IDPs), or proteins that do not fold into stable structures in solution. Our focus is the self-
association of IDPs that occur on high-affinity surfaces (such as microtubules or organelle membranes). Surfaces
can promote self-association by increasing the local IDP concentration and templating IDP conformations more
susceptible to self-association. However, both IDPs and their respective high-affinity surfaces are subject to
numerous cellular modifications, dramatically expanding the experimental parameter space necessary to
precisely characterize this phenomenon. Understanding how self-association is controlled in this space could be
central to understanding their function in physiology and disease. Thus, our laboratory will adapt novel tools
beyond traditional molecular biology to recreate conditions in two model systems where this phenomenon
occurs: Tau condensation on microtubules and α-synuclein multimerization on synaptic vesicle membranes. Not
only does the PI have extensive expertise with biophysically characterizing these IDPs, but the importance of
Tau and α-synuclein to neurobiology and neurodegenerative disease provide a rich history of experimental
insights that can be applied towards this phenomenon. Combined, this expertise and background can be
incorporated into the phenomenon of surface-templated self-association of these IDPs. Furthermore, we will
establish protocols/methods that can be easily exported to study other IDPs that undergo surface-templated self-
association, as well. Overall, our intention by precisely understanding phenomena associated with select IDPs
is to create generalizable mechanisms by which other IDPs behave, eventually providing a rigorous framework
that has explanatory and predictive power for these proteins. By undertaking the proposed research, we hope to
transition our purely biophysics laboratory to an entirely multidisciplinary program that connects protein behavior
to cellular phenomenon.

## Key facts

- **NIH application ID:** 10715794
- **Project number:** 1R35GM150716-01
- **Recipient organization:** UNIVERSITY OF SOUTHERN CALIFORNIA
- **Principal Investigator:** Peter J Chung
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2023
- **Award amount:** $413,864
- **Award type:** 1
- **Project period:** 2023-09-15 → 2028-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10715794

## Citation

> US National Institutes of Health, RePORTER application 10715794, The molecular determinants of surface-templated self-association of intrinsically disordered proteins (1R35GM150716-01). Retrieved via AI Analytics 2026-05-26 from https://api.ai-analytics.org/grant/nih/10715794. Licensed CC0.

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