Impact of Solvents on the Structure of Temporin L Peptide Investigated by Mass Spectrometry
Disciplines
Biochemistry | Medicinal-Pharmaceutical Chemistry
Abstract (300 words maximum)
Over the past decade, pharmaceutical companies have introduced peptide therapeutics that fight a wide range of diseases, such as cancer, diabetes, bacterial diseases, and more. Temporin-L, extracted from frog skin excretion, is an antimicrobial peptide that is active against Gram-negative bacteria and yeast strains. However, Temporin-L is an extremely hydrophobic peptide and has poor solubility with water and partially soluble in organic solvents. Moreover, when Temporin is dissolved in water they do not show stable secondary structure. In this study, we explore the structural and conformational changes of Temporin L by probing the folding and unfolding states in various organic solvents using high resolution mass spectrometry. Peptide samples were prepared with dimethyl sulfoxide (DMSO), methanol (MeOH), trifluoro-ethanol (TFE) at various percentages from 10% to 90%. When Temporin L was dissolved with 10% percentage of solvents, two distinct charge states (2+ and 3+) were noticed. The highest ion current was observed for 3+ charge state in TFE compared to DMSO and MeOH. This indicates that TFE preserves the unfolded state of the Temporin L due to the liner helical structure. At 50% of solvents, a similar trend was observed where 3+ charge states showed the higher ion current compared to 2+ charge states. Interestingly, when Temporin L was dissolved with 90% of solvents, the highest ion current was detected for 2+ charge state which reveals that peptide is in the folded state, but it lost the helical structure.
Academic department under which the project should be listed
CSM - Chemistry and Biochemistry
Primary Investigator (PI) Name
Mohammad Halim
Impact of Solvents on the Structure of Temporin L Peptide Investigated by Mass Spectrometry
Over the past decade, pharmaceutical companies have introduced peptide therapeutics that fight a wide range of diseases, such as cancer, diabetes, bacterial diseases, and more. Temporin-L, extracted from frog skin excretion, is an antimicrobial peptide that is active against Gram-negative bacteria and yeast strains. However, Temporin-L is an extremely hydrophobic peptide and has poor solubility with water and partially soluble in organic solvents. Moreover, when Temporin is dissolved in water they do not show stable secondary structure. In this study, we explore the structural and conformational changes of Temporin L by probing the folding and unfolding states in various organic solvents using high resolution mass spectrometry. Peptide samples were prepared with dimethyl sulfoxide (DMSO), methanol (MeOH), trifluoro-ethanol (TFE) at various percentages from 10% to 90%. When Temporin L was dissolved with 10% percentage of solvents, two distinct charge states (2+ and 3+) were noticed. The highest ion current was observed for 3+ charge state in TFE compared to DMSO and MeOH. This indicates that TFE preserves the unfolded state of the Temporin L due to the liner helical structure. At 50% of solvents, a similar trend was observed where 3+ charge states showed the higher ion current compared to 2+ charge states. Interestingly, when Temporin L was dissolved with 90% of solvents, the highest ion current was detected for 2+ charge state which reveals that peptide is in the folded state, but it lost the helical structure.