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Article

The Conformational Landscape of AlphaFold2-Predicted Amyloidogenic Light Chains and Their Correlation With VL Domain Mutations and Aggregation Propensity.

Journal of molecular recognition : JMR - 1 Sept 2025

Puri Sarita, Chaudhary Ishaan, Khatri Arnav, Patel Basudha, Kumawat Amit, Palkar Sharvari, Das Gourab, Venkatraman Prasanna

Abstract excerpt

Systemic light-chain amyloidosis (AL) is caused by the misfolding and aggregation of immunoglobulin light chains (LCs), which natively form homodimers comprising variable (VL) and constant (CL) domains in each monomer. High sequence variability, particularly within the VL domain, results in varied structural changes and aggregation propensities, making it challenging to develop broadly effective native protein...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 40889878
DOI: 10.1002/jmr.70011

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

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