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Molecular Evidence of Structural Changes in Silk Using Unlimited Degradation Mass Spectrometry

Jie Zhou, Xiong Zhou, Lindan Pan, Yefeng Deng, Hailing Zheng, Zhiqin Peng, Junmin Wan, Yang Zhou, Bing Wang

2023ACS Omega12 citationsDOIOpen Access PDF

Abstract

Proteomics has important uses in archeological science because it can distinguish species, reveal the evolution of paleontology, and provide biological evidence of historical events. However, this technique still has full potential in the study of silk aging mechanisms. In this work, we propose a strategy combining unlimited degradation with mass-spectrometry-based proteomics techniques, which interpret protein fragmentation propensity and secondary structure changes by detecting content changes of specific peptide groups in complex proteomes. This approach was employed to study the conformational changes in silk microscopic crystals after heat treatment. Combining conventional mechanics and crystallographic characterization, a thermal aging degradation mechanism model was proposed. At the same time, it explained the interesting problem that the crystallinity remained unchanged, but the mechanical properties decreased significantly. Focusing on the unlimited degradation process, this method will be widely applicable to the study of silk and wool aging processes and regenerated silk fibroin.

Topics & Concepts

FibroinSILKCrystallinityDegradation (telecommunications)Mass spectrometryProteomeFragmentation (computing)Characterization (materials science)ProteomicsChemistryMechanism (biology)Materials scienceNanotechnologyBiologyComputer scienceCrystallographyChromatographyEcologyPhysicsComposite materialBiochemistryQuantum mechanicsTelecommunicationsGeneSilk-based biomaterials and applicationsAntimicrobial Peptides and ActivitiesInvertebrate Immune Response Mechanisms
Molecular Evidence of Structural Changes in Silk Using Unlimited Degradation Mass Spectrometry | Litcius