aspartyl-aspartic-acid and aspartyltyrosine

aspartyl-aspartic-acid has been researched along with aspartyltyrosine* in 2 studies

Other Studies

2 other study(ies) available for aspartyl-aspartic-acid and aspartyltyrosine

Article	Year
Active sites of peptides Asp-Asp-Asp-Tyr and Asp-Tyr-Asp-Asp protect against cellular oxidative stress. Food chemistry, 2022, Jan-01, Volume: 366 The protective effects of the peptides Asp-Asp-Asp-Tyr (DDDY) and Asp-Tyr-Asp-Asp (DYDD) against AAPH-induced HepG2 cells are unclear. Our objective was to investigate the active sites of these peptides and their cellular antioxidant mechanism. DDDY and DYDD show a direct free radical scavenging effect in reducing ROS levels and maintained cellular antioxidant enzymes at normal levels. The quantum chemistry analysis of the electronic properties of antioxidant activity showed that DYDD has a greater energy in the highest occupied molecular orbital than DDDY, and O Topics: Antioxidants; Catalytic Domain; Dipeptides; Oxidative Stress; Peptides	2022
Mechanisms underlying the antimicrobial actions of the antimicrobial peptides Asp-Tyr-Asp-Asp and Asp-Asp-Asp-Tyr. Food research international (Ottawa, Ont.), 2021, Volume: 139 The peptides Asp-Tyr-Asp-Asp (DYDD) and Asp-Asp-Asp-Tyr (DDDY) extracted from Dendrobium aphyllum have antimicrobial effects on Escherichia coli, Pseudomonas aeruginosa, and Monilia albicans, but no effects on Bacillus subtilis and Staphylococcus aureus. The effects of a hydrophobic environment on the secondary structures of these molecules were determined using circular dichroism and atomic force microscopy. Although scanning electron microscopy revealed that DDDY was more destructive to membranes than DYDD, both peptides showed antimicrobial effects against three pathogens. The minimum inhibitory concentration (MIC) of DYDD (18.075 mg/mL) against E. coli was higher than that of DDDY (4.519 mg/mL), and the influence of DYDD on the cell surface potential energy of E. coli was also greater (a decrease of 6.4 ± 0.66 mV) than that of DDDY (a decrease of 4.37 ± 0.77 mV). Moreover, the cell membrane damage and content leakage of DYDD-treated E. coli cells were more severe than those observed in the DDDY-treated cells. However, DDDY showed stronger antibacterial activity against P. aeruginosa and M. albicans than DYDD. A molecular dynamic simulation revealed that the mechanisms underlying the interaction between these two peptides and lipid bilayers were remarkably different. Therefore, two separate models were proposed to describe their antimicrobial activities. Topics: Amino Acid Sequence; Anti-Infective Agents; Antimicrobial Cationic Peptides; Dipeptides; Escherichia coli; Pore Forming Cytotoxic Proteins	2021

Article

Year

Active sites of peptides Asp-Asp-Asp-Tyr and Asp-Tyr-Asp-Asp protect against cellular oxidative stress.

Food chemistry, 2022, Jan-01, Volume: 366

The protective effects of the peptides Asp-Asp-Asp-Tyr (DDDY) and Asp-Tyr-Asp-Asp (DYDD) against AAPH-induced HepG2 cells are unclear. Our objective was to investigate the active sites of these peptides and their cellular antioxidant mechanism. DDDY and DYDD show a direct free radical scavenging effect in reducing ROS levels and maintained cellular antioxidant enzymes at normal levels. The quantum chemistry analysis of the electronic properties of antioxidant activity showed that DYDD has a greater energy in the highest occupied molecular orbital than DDDY, and O

Topics: Antioxidants; Catalytic Domain; Dipeptides; Oxidative Stress; Peptides

2022

Mechanisms underlying the antimicrobial actions of the antimicrobial peptides Asp-Tyr-Asp-Asp and Asp-Asp-Asp-Tyr.

Food research international (Ottawa, Ont.), 2021, Volume: 139

The peptides Asp-Tyr-Asp-Asp (DYDD) and Asp-Asp-Asp-Tyr (DDDY) extracted from Dendrobium aphyllum have antimicrobial effects on Escherichia coli, Pseudomonas aeruginosa, and Monilia albicans, but no effects on Bacillus subtilis and Staphylococcus aureus. The effects of a hydrophobic environment on the secondary structures of these molecules were determined using circular dichroism and atomic force microscopy. Although scanning electron microscopy revealed that DDDY was more destructive to membranes than DYDD, both peptides showed antimicrobial effects against three pathogens. The minimum inhibitory concentration (MIC) of DYDD (18.075 mg/mL) against E. coli was higher than that of DDDY (4.519 mg/mL), and the influence of DYDD on the cell surface potential energy of E. coli was also greater (a decrease of 6.4 ± 0.66 mV) than that of DDDY (a decrease of 4.37 ± 0.77 mV). Moreover, the cell membrane damage and content leakage of DYDD-treated E. coli cells were more severe than those observed in the DDDY-treated cells. However, DDDY showed stronger antibacterial activity against P. aeruginosa and M. albicans than DYDD. A molecular dynamic simulation revealed that the mechanisms underlying the interaction between these two peptides and lipid bilayers were remarkably different. Therefore, two separate models were proposed to describe their antimicrobial activities.

Topics: Amino Acid Sequence; Anti-Infective Agents; Antimicrobial Cationic Peptides; Dipeptides; Escherichia coli; Pore Forming Cytotoxic Proteins

2021