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Cell Penetrability of a γ-Crystallin Peptide Fragment from the Discarded Cataractous Eye Emulsion.

ABSTRACT: The efficiency of the intracellular transport of medication and target specificity is frequently hampered by biological obstacles. The potential for therapeutic use of peptide fragments from naturally occurring proteins is promising, as peptides exhibit high selectivity due to several possibilities of interaction with their target. Certain peptide sequences, often referred to as cell-penetrating peptides (CPPs), are those that can penetrate cell membranes. Our goal is to find these sequences in the discarded postcataractery surgery emulsion known as the cataractous eye protein isolate (CEPI). One peptide fragment from this discarded protein has been identified to be a potential CPP based on the similarities with other well-known CPPs. Cell membrane penetrability and cytotoxicity of the peptide have been investigated. Fibroblast cells were incubated with the fluorescently labeled peptide and were observed under fluorescence as well as under confocal microscopy. It was found that the peptide possesses a cell-penetrating ability.

SUBMITTER: Chowdhury P

PROVIDER: S-EPMC10993246 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature

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Cell Penetrability of a γ-Crystallin Peptide Fragment from the Discarded Cataractous Eye Emulsion.

Chowdhury Prasun P Ojha Atul Kumar AK Bhowmik Shishir S Halder Krishna K Sabnam Kabira K Santra Sujan S Chaudhury Koel K Dasgupta Swagata S

ACS omega 20240306 13

The efficiency of the intracellular transport of medication and target specificity is frequently hampered by biological obstacles. The potential for therapeutic use of peptide fragments from naturally occurring proteins is promising, as peptides exhibit high selectivity due to several possibilities of interaction with their target. Certain peptide sequences, often referred to as cell-penetrating peptides (CPPs), are those that can penetrate cell membranes. Our goal is to find these sequences in ...[more]

PMID: 38585046

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Project description:PURPOSE: Post-translational modification (PTM) of lens proteins is believed to play various roles in age-related lens function and development. Among the different types of PTM, phosphorylation is most noteworthy to play a major role in the regulation of various biosignaling pathways in relation to metabolic processes and cellular functions. The present study reported the quantitative analysis of the in vivo phosphoproteomics profiles of human normal and cataractous lenses with the aim of identifying specific phosphorylation sites which may provide insights into the physiologic significance of phosphorylation in relation to cataract formation. METHODS: To improve detection sensitivity of low abundant proteins, we first adopted SDS-gel electrophoresis fractionation of lens extracts to identify and compare the protein compositions between normal and cataractous lenses, followed by tryptic digestion, enrichment of phosphopeptides by immobilized metal affinity chromatography (IMAC) and nano-liquid chromatography coupled tandem mass spectrometry (nanoLC-MS/MS) analysis. RESULTS: By comprehensively screening of the phosphoproteome in normal and cataractous lenses, we identified 32 phosphoproteins and 73 phosphorylated sites. The most abundantly phosphorylated proteins are two subunits of ?-crystallin, i.e., ?B1-crystallin (12%) and ?B2-crystallin (12%). Moreover, serine was found to be the most abundantly phosphorylated residue (72%) in comparison with threonine (24%) and tyrosine (4%) in the lens phosphoproteome. The quantitative analysis revealed significant and distinct changes of 19 phosphoproteins corresponding to 28 phosphorylated sites between these two types of human lenses, including 20 newly discovered novel phosphorylation sites on lens proteins. CONCLUSIONS: The shotgun phosphoproteomics approach to characterize protein phosphorylation may be adapted and extended to the comprehensive analysis of other types of post-translational modification of lens proteins in vivo. The identification of these novel phosphorylation sites in lens proteins that showed differential expression in the cataractous lens may bear some unknown physiologic significance and provide insights into phosphorylation-related human eye diseases, which warrant further investigation in the future.

Dataset Information

Cell Penetrability of a γ-Crystallin Peptide Fragment from the Discarded Cataractous Eye Emulsion.

Publications

Cell Penetrability of a γ-Crystallin Peptide Fragment from the Discarded Cataractous Eye Emulsion.

Similar Datasets

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