Cataract has been the primary factor causing blindness in nearly 80% of the elderly generation around the world. Crystallin protein in the eye lens aggregation initial the cataract particularly peptide sequence 66-80 in α subunit. Many patients struggle to experience surgical procedures due to financial and medical restrictions. An urge to develop a drug to cure cataracts will have dramatically increased. The advancement of MS-based therapeutic drug development shows promising outcomes for many diseases. In this study, we focus on two synthetic macromolecules known as Host A, and B that show noncovalent interactions with α 66-80 crystallin peptide chain and prevent aggregation. The main objective of this study was to evaluate the coordination of α 66-80 peptides to the synthetic macrocyclic host molecule A and B by ESI-MS. The 1:1 host: peptide complexes were detected by ESI-MS. The host: peptide competition reactions were also carried out in order to gain insight into the relative binding affinities of hosts. Understanding the reactivity of the host molecules with peptide structure and fragmentation pattern is of great importance for developing improved therapeutic treatment against cataract-related peptide aggregation, and replacing cataract eye lens surgery.

Mass spectrometry analysis of the host-peptide complexes: Towards new therapies against cataracts

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ACS Fall 2022

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