A machine learning protocol for predicting structural distributions of amyloid-forming proteins from 2D IR spectra.

ABSTRACT: Protein misfolding plays a central role in diseases such as Alzheimer's disease, Parkinson's disease, type 2 diabetes, and transthyretin amyloidosis (ATTR), often driven by specific aggregation-prone segments such as Aβ_17-23 and Aβ_37-42 of amyloid-β42 (Aβ42), α-Syn_66-74 and α-Syn_71-82 of α-synuclein (α-syn), hIAPP_22-27 of human islet amyloid polypeptide (hIAPP), and TTR_105-115 of transthyretin (TTR). Capturing the atomic-level structural features of these transient and dynamically fluctuating regions remains challenging. Two-dimensional infrared (2DIR) spectroscopy provides rich vibrational fingerprints that are highly sensitive to protein conformational dynamics, but e

SUBMITTER: Ye S 

PROVIDER: S-EPMC12685097 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature