Protein aggregation as a consequence of non-enzymatic glycation: Therapeutic intervention using aspartic acid and arginine
| Autor: | Anna Feroz, Mohd Sajid Khan, Bilqees Bano, Peerzada Shariq Shaheen Khaki |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Glycosylation
Arginine Ribose 02 engineering and technology Protein aggregation Biochemistry Fluorescence 03 medical and health sciences chemistry.chemical_compound Protein Aggregates Structural Biology Glycation Aspartic acid Chromatin structure remodeling (RSC) complex Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Aspartic Acid biology Circular Dichroism Proteins General Medicine 021001 nanoscience & nanotechnology Amino acid Glucose Spectrometry Fluorescence chemistry biology.protein Thioflavin 0210 nano-technology Mustard Plant |
| Zdroj: | International journal of biological macromolecules. 163 |
| ISSN: | 1879-0003 |
| Popis: | Non-enzymatic glycation tempted AGEs of proteins are currently at the heart of a number of pathological conditions. Production of chemically stable AGEs can permanently alter the protein structure and function, concomitantly leading to dilapidated situations. Keeping in perspective, present study aims to report the glycation induced structural and functional modification of a cystatin type isolated from rai mustard seeds, using RSC-glucose and RSC-ribose as model system. Among the sugars studied, ribose was found to be most potent glycating agent as evident from different biophysical assays. During the course of incubation, RSC was observed to pass through a series of structural intermediates as revealed by circular dichroism, altered intrinsic fluorescence and high ANS binding. RSC incubation with ribose post day 36 revealed the possible buildup of β structures as observed in CD spectral analysis, hinting towards the generation of aggregated structures in RSC. High thioflavin T fluorescence and increased Congo red absorbance together with enhanced turbidity of the modified form confirmed the aggregation of RSC. The study further revealed anti-glycation and anti-aggregation potential of amino acids; aspartic acid and arginine as they prevented and/or slowed down the process of AGEs and β structure buildup in a concentration dependent manner with arginine proving to be the most effective one. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect