**Author Listing - Lead/ Submitting Author (we will be communicating with this individual): Name, Institution, City and State where the work was done. Co-authors will be added in a separate section.**
Julie Courraud, Dep. of Clinical Therapeutics, School of Medicine, & Laboratory of Analytical Chemistry, Dep. of Chemistry, National and Kapodistrian University of Athens, Alexandra Hospital, Athens, Greece

**Main Body of the Abstract**
Background: Typing of amyloid proteins by mass spectrometry represents the first clinical application of proteomics in diagnostics. Since the initial method was published ~15 years ago, numerous centers worldwide have adopted similar techniques.
Purpose: At the Referral Center of Amyloidosis in Greece, our objectives were to 1) establish proteomic typing of amyloid proteins for diagnostic purposes and 2) explore the benefits of employing library-free Data-Independent Acquisition (DIA) to simultaneously address research questions.
Methods: We recently implemented a proteomic analysis (Canetti et al., 2020) of laser-microdissected amyloid depots using nano LC coupled with a timsTOF fleX mass spectrometer. Over one hundred paraffin-embedded biopsies from various tissues, including subcutaneous fat, kidney, salivary gland, lung, and heart, were analyzed. Leveraging the capabilities of Parallel Accumulation–Serial Fragmentation (PASEF) technology, we routinely utilize library-free DIA, expanding protein detection from the typical ~100 protein groups in Data-Dependent Acquisition (DDA) to 800+.
Results: This presentation outlines the challenges associated with establishing such an assay for newcomers and our validation approach in a clinical setting. Following successful replication of diagnostic results from 14 fat tissue biopsies of patients with various AL, as analyzed by the UK National Amyloidosis Centre in London, we are continually expanding our internal validation cohort. The increased sensitivity that has been achieved aids diagnostics in cases of scarce deposition and allows for better characterization of tissue substructures' proteomes for research purposes. Capitalizing on the data, we are exploring the spatial distribution of proteins, as well as new patterns of potential diagnostic and/or prognostic value.



**Author Listing - Lead/ Submitting Author (we will be communicating with this individual): Name, Institution, City and State where the work was done. Co-authors will be added in a separate section.**
**Julie Courraud**, Dep. of Clinical Therapeutics, School of Medicine, & Laboratory of Analytical Chemistry, Dep. of Chemistry, National and Kapodistrian University of Athens, Alexandra Hospital, Athens, Greece

**Main Body of the Abstract**
**Background:** Typing of amyloid proteins by mass spectrometry represents the first clinical application of proteomics in diagnostics. Since the initial method was published ~15 years ago, numerous centers worldwide have adopted similar techniques.
**Purpose:** At the Referral Center of Amyloidosis in Greece, our objectives were to 1) establish proteomic typing of amyloid proteins for diagnostic purposes and 2) explore the benefits of employing library-free Data-Independent Acquisition (DIA) to simultaneously address research questions.
**Methods:** We recently implemented a proteomic analysis (Canetti et al., 2020) of laser-microdissected amyloid depots using nano LC coupled with a timsTOF fleX mass spectrometer. Over one hundred paraffin-embedded biopsies from various tissues, including subcutaneous fat, kidney, salivary gland, lung, and heart, were analyzed. Leveraging the capabilities of Parallel Accumulation–Serial Fragmentation (PASEF) technology, we routinely utilize library-free DIA, expanding protein detection from the typical ~100 protein groups in Data-Dependent Acquisition (DDA) to 800+.
**Results:** This presentation outlines the challenges associated with establishing such an assay for newcomers and our validation approach in a clinical setting. Following successful replication of diagnostic results from 14 fat tissue biopsies of patients with various AL, as analyzed by the UK National Amyloidosis Centre in London, we are continually expanding our internal validation cohort. The increased sensitivity that has been achieved aids diagnostics in cases of scarce deposition and allows for better characterization of tissue substructures' proteomes for research purposes. Capitalizing on the data, we are exploring the spatial distribution of proteins, as well as new patterns of potential diagnostic and/or prognostic value.



Setting up proteomic typing from scratch in Greece: challenges and opportunities PA71 (#380)

We invite you to attend the XIX International Symposium on Amyloidosis to be held in Rochester, MN.

This symposium is organized as a hybrid meeting (with the focus on in-person) held from Sunday, May 26 through Thursday, May 30, 2024.

Together with the ISA Board and members of Mayo Clinic, a very attractive scientific hybrid program is being planned. The program will cover a variety of types of systemic amyloidosis: ATTR (hereditary and wild-type), AL (light-chain), AA and less frequent forms. There will be key lectures, specific symposia including those company sponsored, oral presentations and poster sessions of accepted abstracts.

COURSE DESCRIPTION
This program will provide a comprehensive review of state-of-the-art education in systemic amyloidosis: basic science, pathophysiology, diagnosis, current and emerging treatments. Scientific presentations will include competitive oral and poster abstracts. The rapid evolution of scientific discovery and expanding treatment options has created tremendous interest in the field and this meeting will fill and important gap in educating scientists and clinicians.