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Updated: Aug 30, 2026
Spectrophotometric Determination of Phycobiliprotein Content in Cyanobacterium Synechocystis
Published on: September 11, 2018
Phycocyanobilin: A potential bioactive compound from Arthrospira platensis targeting LYN protein associated with
Amnart Chaiprasert1,2, Ping Han3,4, Teeraphan Laomettachit3
1Biotechnology Program, School of Bioresources and Technology (SBT), King Mongkut's University of Technology Thonburi (KMUTT), Bangkok, Thailand.
Abstract:
Phycocyanobilin, a bioactive compound derived from Arthrospira platensis C1, was investigated for its potential role in systemic lupus erythematosus (SLE) based on its structural similarity to bilirubin, with a Tanimoto score of 93%. Molecular docking revealed favorable binding affinities between phycocyanobilin and several protein targets, including EGFR, FYN, HLA-B, LCK, LYN, and TP53. Target prediction further identified LYN kinase as a key candidate. Molecular dynamics simulations demonstrated stable binding of the phycocyanobilin-LYN complex, with interaction profiles comparable to those of the native ligand, staurosporine. Binding free energy and residue-level analyses supported strong and stable interactions, highlighting key contributions to complex stability. Overall, these findings provide mechanistic insight into the interaction between phycocyanobilin and LYN, suggesting that this compound may modulate LYN-associated signaling pathways and warrants further investigation in the context of SLE.